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PDBsum entry 5lab

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protein ligands metals links
Hydrolase PDB id
5lab

 

 

 

 

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Contents
Protein chain
159 a.a.
Ligands
NGH
Metals
_ZN ×2
_CA ×3
Waters ×236
PDB id:
5lab
Name: Hydrolase
Title: Crystal structure of the catalytic domain of human mmp12 complexed with the inhibitor nngh
Structure: Macrophage metalloelastase. Chain: a. Fragment: unp residues 106-263. Synonym: mme,macrophage elastase,hme,matrix metalloproteinase-12,mmp- 12. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mmp12, hme. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
Resolution:
1.34Å     R-factor:   0.158     R-free:   0.195
Authors: E.Ravera,V.Calderone,C.Luchinat
Key ref: L.Benda et al. First-Principles calculation of pseudo-Contact shifts paramagnetic metalloprotein. To be published, . PubMed id: 27781358
Date:
14-Jun-16     Release date:   10-Aug-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P39900  (MMP12_HUMAN) -  Macrophage metalloelastase from Homo sapiens
Seq:
Struc:
470 a.a.
159 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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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