Structure of PDB 3shi Chain G

Receptor sequence
>3shiG (length=156) Species: 9606 (Homo sapiens) [Search protein sequence]
NPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEG
QADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTN
NFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDG
IQAIYG
3D structure
PDB3shi The catalytic domain of MMP-1 studied through tagged lanthanides.
ChainG
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H218 H222 H228
Catalytic site (residue number reindexed from 1) H113 H117 H123
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 G H218 H222 H228 H113 H117 H123
BS02 ZN G H168 D170 H183 H196 H63 D65 H78 H91
BS03 CA G D175 G176 G178 N180 D198 E201 D70 G71 G73 N75 D93 E96
BS04 CA G D124 E199 E201 D19 E94 E96
BS05 CA G D158 G190 G192 D194 D53 G85 G87 D89
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3shi, PDBe:3shi, PDBj:3shi
PDBsum3shi
PubMed21945315
UniProtP03956|MMP1_HUMAN Interstitial collagenase (Gene Name=MMP1)

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