Structure of PDB 966c Chain A

Receptor sequence
>966cA (length=157) Species: 9606 (Homo sapiens) [Search protein sequence]
RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQA
DIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNF
REYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQ
AIYGRSQ
3D structure
PDB966c Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H111 E112 H115 H121
Enzyme Commision number 3.4.24.7: interstitial collagenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A H218 H222 H228 H111 H115 H121
BS02 ZN A H168 D170 H183 H196 H61 D63 H76 H89
BS03 CA A D175 G176 P177 G178 N180 D198 E201 D68 G69 P70 G71 N73 D91 E94
BS04 CA A D158 G190 G192 D194 D51 G83 G85 D87
BS05 CA A D124 E199 E201 D17 E92 E94
BS06 RS2 A N180 L181 H218 E219 H222 H228 L235 Y237 S239 T241 N73 L74 H111 E112 H115 H121 L128 Y130 S132 T134 MOAD: Ki=23nM
PDBbind-CN: -logKd/Ki=7.64,Ki=23nM
BindingDB: Ki=23nM
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0031012 extracellular matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:966c, PDBe:966c, PDBj:966c
PDBsum966c
PubMed10074939
UniProtP03956|MMP1_HUMAN Interstitial collagenase (Gene Name=MMP1)

[Back to BioLiP]