_EC 3.4.24.27 Thermolysin. 125 PDB entries  
EC 3.-.-.- Hydrolases. [21,051 PDB entries]
EC 3.4.-.- Acting on peptide bonds (peptide hydrolases). [6,852 PDB entries]
EC 3.4.24.- Metalloendopeptidases. [610 PDB entries]
EC 3.4.24.27 Thermolysin. [125 PDB entries]    
1fj3

Reaction: Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.
Other name(s): Bacillus thermoproteolyticus neutral proteinase.
Cofactor(s): Ca(2+); Zn(2+).
Comments: A thermostable extracellular metalloendopeptidase containing four calcium ions. Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus and Aspergillus oryzae. Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin. Belongs to peptidase family M4. Formerly Ec 3.4.24.4.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 125 PDB entries in enzyme class E.C.3.4.24.27

  PDB code Protein
1fj3
Thermolysin (50% acetone soaked)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1fjo
Thermolysin (60% acetone soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1fjq
Thermolysin (70% acetone soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1fjt
Thermolysin (50% acetonitrile soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1fju
Thermolysin (80% acetonitrile soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1fjv
Thermolysin (60% acetonitrile soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1fjw
Thermolysin (50 mm phenol soaked)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1gxw
The 2.2 a resolution structure of thermolysin crystallized in presence of potassium thiocyanate
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1hyt
Re-determination and refinement of the complex of benzylsucc with thermolysin and its relation to the complex with carboxypeptidase a
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1kei
Thermolysin (substrate-free)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1kjo
Thermolysin complexed with z-l-threonine (benzyloxycarbonyl- threonine)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1kjp
Thermolysin complexed with z-l-glutamic acid (benzyloxycarbo glutamic acid)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1kkk
Thermolysin complexed with z-l-aspartic acid (benzyloxycarbo aspartic acid)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1kl6
Thermolysin complexed with z-l-alanine (benzyloxycarbonyl-l-
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1kr6
Thermolysin complexed with z-d-glutamic acid (benzyloxycarbo glutamic acid)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1kro
Thermolysin complexed with z-d-threonine (benzyloxycarbonyl- threonine)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1ks7
Thermolysin complexed with z-d-aspartic acid (benzyloxycarbo aspartic acid)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1kto
Thermolysin complexed with z-d-alanine (benzyloxycarbonyl-d-
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1l3f
Thermolysin in the absence of substrate has an open conformation
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1lna
A structural analysis of metal substitutions in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1lnb
A structural analysis of metal substitutions in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1lnc
A structural analysis of metal substitutions in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1lnd
A structural analysis of metal substitutions in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1lne
A structural analysis of metal substitutions in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1lnf
A structural analysis of metal substitutions in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1no0
Thermolysin with an alpha-amino phosphinic inhibitor
Source: Bacillus thermoproteolyticus. Bacteria
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1os0
Thermolysin with an alpha-amino phosphinic inhibitor
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1pe5
Thermolysin with tricyclic inhibitor
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1pe7
Thermolysin with bicyclic inhibitor
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1pe8
Thermolysin with monocyclic inhibitor
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1qf0
Thermolysin (E.C.3.4.24.27) complexed with (2-sulphanyl-3- phenylpropanoyl)-phe-tyr. Parameters for zn-bidentation of mercaptoacyldipeptides in metalloendopeptidase
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1qf1
Thermolysin (E.C.3.4.24.27) complexed with (2- sulphanylheptanoyl)-phe-ala. Parameters for zn-bidentation of mercaptoacyldipeptides in metalloendopeptidase
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1qf2
Thermolysin (E.C.3.4.24.27) complexed with (2-sulphanyl-3- phenylpropanoyl)-gly-(5-phenylproline). Parameters for zn- monodentation of mercaptoacyldipeptides in metalloendopeptidase
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1thl
Thermolysin complexed with a novel glutaramide derivative, n s)-carboxy-4-phenylbutyl) cyclopentylcarbonyl)-(s)-tryptoph
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1tli
Thermolysin (2% isopropanol soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1tlp
Crystallographic structural analysis of phosphoramidates as and transition-state analogs of thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1tlx
Thermolysin (native)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1tmn
Binding of n-carboxymethyl dipeptide inhibitors to thermolys determined by x-ray crystallography. A novel class of trans state analogues for zinc peptidases
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427. Gene: npr
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1trl
Nmr solution structure of thE C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chains: A, B (62 residues) CATH domain: 1.10.390.10
1y3g
Crystal structure of a silanediol protease inhibitor bound to thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1z9g
Crystal structure analysis of thermolysin complexed with the inhibitor (r)-retro-thiorphan
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
1zdp
Crystal structure analysis of thermolysin complexed with the inhibitor (s)-thiorphan
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
2a7g
On the routine use of soft x-rays in macromolecular crystall part iii- the optimal data collection wavelength
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
2g4z
Anomalous substructure of thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
2tli
Thermolysin (5% isopropanol soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
2tlx
Thermolysin (native)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
2tmn
Crystallographic structural analysis of phosphoramidates as and transition-state analogs of thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
2whz
Dipeptide inhibitors of thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
2wi0
Dipeptide inhibitors of thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3dnz
Thermolysin by lb nanotemplate method before high x-ray dose on esrf id14-2 beamline
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3do0
Thermolysin by classical hanging drop method after high x- ray dose on esrf id14-2 beamline
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3do1
Thermolysin by classical hanging drop method before high x- ray dose on esrf id14-2 beamline
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3do2
Thermolysin by lb nanotemplate method after high x-ray dose on esrf id14-2 beamline
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3eim
Metal exchange in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3f28
Thermolysin inhibition
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3f2p
Thermolysin inhibition
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3fb0
Metal exchange in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3fbo
Metal exchange in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3fcq
Thermolysin inhibition
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3fgd
Drugscore fp: thermoylsin in complex with fragment.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3flf
Thermolysin inhibition
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3for
Thermolysin complexed with bnpa (2-benzyl-3-nitro propanoic acid amide)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427. Strain: rokko
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3fv4
Thermolysin inhibition
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3fvp
Thermolysin inhibition
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3fwd
Thermolysin inhibition
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3fxp
Thermolysin inhibition
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3fxs
Metal exchange in thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3ls7
Crystal structure of thermolysin in complex with xenon
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3ms3
Crystal structure of thermolysin in complex with aniline
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3msa
Crystal structure of thermolysin in complex with 3-bromophen
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3msf
Crystal structure of thermolysin in complex with urea
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3msn
Crystal structure of thermolysin in complex with n-methylure
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3n21
Crystal structure of thermolysin in complex with s-1,2-propa
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3nn7
Crystal structure of thermolysin in complex with 2-bromoacet
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3p7p
Radiation damage study of thermolysin - 100k structure a (0.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3p7q
Radiation damage study of thermolysin - 100k structure b (2.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3p7r
Radiation damage study of thermolysin - 100k structurE C (4.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3p7s
Radiation damage study of thermolysin - 100k structure d (7.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3p7t
Radiation damage study of thermolysin - 160k structure a (0.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3p7u
Radiation damage study of thermolysin - 160k structure b (2.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3p7v
Radiation damage study of thermolysin - 160k structurE C (4.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3p7w
Radiation damage study of thermolysin - 160k structure d (7.
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3qgo
Structure of thermolysin in complex with l-phenylalanine met
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3qh1
Structure of thermolysin in complex with n-benzyloxycarbonyl aspartic acid
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3qh5
Structure of thermolysin in complex with n-carbobenzyloxy-l- acid and l-phenylalanine methyl ester
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3ssb
Structure of insect metalloproteinase inhibitor in complex w thermolysin
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427. Galleria mellonella. Greater wax moth. Organism_taxid: 7137. Gene: impi. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t2h
Tetragonal thermolysin in the presence of tmao
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t2i
Tetragonal thermolysin in the presence of sarcosine
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t2j
Tetragonal thermolysin in the presence of betaine
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t73
Thermolysin in complex with ubtln22
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t74
Thermolysin in complex with ubtln27
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t87
Thermolysin in complex with ubtln28
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t8c
Thermolysin in complex with ubtln30
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t8d
Thermolysin in complex with ubtln31
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t8f
Thermolysin in complex with ubtln34
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t8g
Thermolysin in complex with ubtln26
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3t8h
Thermolysin in complex with ubtln29
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3tli
Thermolysin (10% isopropanol soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3tmn
The binding of l-valyl-l-tryptophan to crystalline thermolys illustrates the mode of interaction of a product of peptide hydrolysis
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
3zi6
Structure of thermolysin solved by sad from data collected b data collection (ddc) using the grob robot goniometer
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4d91
Thermolysin in complex with dmso and acetate
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4d9w
Thermolysin in complex with ubtln32
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4h57
Thermolysin inhibition
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4mtw
Thermolysin in complex with ubtln36
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4mwp
Thermolysin in complex with ubtln46
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4mxj
Thermolysin in complex with ubtln35
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4mzn
Thermolysin in complex with ubtln59
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4n4e
Thermolysin in complex with ubtln58
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4n5p
Thermolysin in complex with ubtln20
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4n66
Thermolysin in complex with ubtln37
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4oi5
Glycerol-free structure of thermolysin in complex with ubtln
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4ow3
Thermolysin structure determined by free-electron laser
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (314 residues) CATH domains: 3.10.170.10 1.10.390.10
4tli
Thermolysin (25% isopropanol soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4tln
Binding of hydroxamic acid inhibitors to crystalline thermol suggests a pentacoordinate zinc intermediate in catalysis
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4tmn
Slow-and fast-binding inhibitors of thermolysin display diff modes of binding. Crystallographic analysis of extended phosphonamidate transition-state analogues
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
4tnl
1.8 a resolution room temperature structure of thermolysin r using an xfel
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (315 residues) CATH domains: 3.10.170.10 1.10.390.10
5tli
Thermolysin (60% isopropanol soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
5tln
Binding of hydroxamic acid inhibitors to crystalline thermol suggests a pentacoordinate zinc intermediate in catalysis
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
5tmn
Slow-and fast-binding inhibitors of thermolysin display diff modes of binding. Crystallographic analysis of extended phosphonamidate transition-state analogues
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
6tli
Thermolysin (60% isopropanol soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
6tmn
Structures of two thermolysin-inhibitor complexes that diffe single hydrogen bond
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10
7tli
Thermolysin (90% isopropanol soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
7tln
Structural analysis of the inhibition of thermolysin by an a site-directed irreversible inhibitor
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
8tli
Thermolysin (100% isopropanol soaked crystals)
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: A (316 residues) CATH domains: 3.10.170.10 1.10.390.10
8tln
Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis
Source: Bacillus thermoproteolyticus. Organism_taxid: 1427
Chain: E (316 residues) CATH domains: 3.10.170.10 1.10.390.10