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PDBsum entry 3uvc

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3uvc

 

 

 

 

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Contents
Protein chains
158 a.a.
Ligands
IMD ×5
_CL ×6
0D2
EDO ×2
Metals
_ZN ×6
_CA ×7
Waters ×505
PDB id:
3uvc
Name: Hydrolase
Title: Mmp12 in a complex with the dimeric adduct: 5-(5-phenylhydantoin)-5- phenylhydantoin
Structure: Macrophage metalloelastase. Chain: a, b. Fragment: catalytic domain, residues 106-263. Synonym: mme, macrophage elastase, me, hme, matrix metalloproteinase- 12, mmp-12. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: 4321, hme, mmp12. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.30Å     R-factor:   0.132     R-free:   0.174
Authors: D.J.Derbyshire,H.Danielson,S.Nystrum
Key ref: H.Nordstrom et al. Characterization of fragments interacting with mmp-12. To be published, .
Date:
29-Nov-11     Release date:   02-Jan-13    
PROCHECK
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 Headers
 References

Protein chains
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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