 |
PDBsum entry 3shi
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Hydrolase
|
|
|
Title:
|
|
Crystal structure of human mmp1 catalytic domain at 2.2 a resolution
|
|
Structure:
|
|
Interstitial collagenase. Chain: a, g, m. Fragment: unp residues 106-261. Synonym: mmp-1, matrix metalloproteinase-1, 22 kda interstitial collagenase, fibroblast collagenase. Engineered: yes
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Gene: mmp1, clg. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
Resolution:
|
|
|
2.20Å
|
R-factor:
|
0.215
|
R-free:
|
0.278
|
|
|
Authors:
|
|
I.Bertini,V.Calderone,L.Cerofolini,M.Fragai,C.F.G.C.Geraldes, P.Hermann,C.Luchinat,G.Parigi,J.Teixeira
|
|
Key ref:
|
|
I.Bertini
et al.
(2012).
The catalytic domain of MMP-1 studied through tagged lanthanides.
Febs Lett,
586,
557-567.
PubMed id:
|
|
|
Date:
|
|
|
16-Jun-11
|
Release date:
|
21-Sep-11
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P03956
(MMP1_HUMAN) -
Interstitial collagenase from Homo sapiens
|
|
|
|
Seq:
Struc:
|
|
|
|
469 a.a.
156 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.3.4.24.7
- interstitial collagenase.
|
|
|
|
|
|
|
Reaction:
|
|
Cleaves preferentially one bond in native collagen. Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
|
|
|
|
|
|
Cofactor:
|
|
Zn(2+)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Febs Lett
586:557-567
(2012)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
The catalytic domain of MMP-1 studied through tagged lanthanides.
|
|
I.Bertini,
V.Calderone,
L.Cerofolini,
M.Fragai,
C.F.Geraldes,
P.Hermann,
C.Luchinat,
G.Parigi,
J.M.Teixeira.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
