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PDBsum entry 3rts

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protein ligands metals links
Hydrolase/hydrolase inhibitor PDB id
3rts

 

 

 

 

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Contents
Protein chain
158 a.a.
Ligands
KLG
Metals
_ZN ×2
_CA ×3
Waters ×151
PDB id:
3rts
Name: Hydrolase/hydrolase inhibitor
Title: Human mmp-12 catalytic domain in complex with N -Hydroxy-2-(2- phenylethylsulfonamido)acetamide
Structure: Macrophage metalloelastase. Chain: a. Fragment: unp residues 106-263. Synonym: mme, macrophage elastase, me, hme, matrix metalloproteinase- 12, mmp-12. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mmp12, hme. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.81Å     R-factor:   0.176     R-free:   0.236
Authors: I.Bertini,V.Calderone,M.Fragai,C.Luchinat,M.Mori,C.Nativi
Key ref: Adidinini et al. Cibibutution of ligand free energy of solvation to de nototenent mmps inhibito.S.. J c chehem, .
Date:
04-May-11     Release date:   04-Jul-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P39900  (MMP12_HUMAN) -  Macrophage metalloelastase from Homo sapiens
Seq:
Struc:
470 a.a.
158 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.4.24.65  - macrophage elastase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.
      Cofactor: Ca(2+); Zn(2+)

 

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