Structure of PDB 1i76 Chain A

Receptor sequence
>1i76A (length=163) Species: 9606 (Homo sapiens) [Search protein sequence]
MLTPGNPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFT
RISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAE
ETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSL
PQDDIDGIQAIYG
3D structure
PDB1i76 Two crystal structures of human neutrophil collagenase, one complexed with a primed- and the other with an unprimed-side inhibitor: implications for drug design.
ChainA
Resolution1.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H197 E198 H201 H207
Catalytic site (residue number reindexed from 1) H118 E119 H122 H128
Enzyme Commision number 3.4.24.34: neutrophil 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 CA A D137 G169 G171 D173 D58 G90 G92 D94
BS02 CA A D154 G155 N157 I159 D177 E180 D75 G76 N78 I80 D98 E101
BS03 ZN A H147 D149 H162 H175 H68 D70 H83 H96
BS04 ZN A H197 H201 H207 H118 H122 H128
BS05 BSI A L160 A161 H197 E198 H201 H207 L214 P217 N218 Y219 L81 A82 H118 E119 H122 H128 L135 P138 N139 Y140
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:1i76, PDBe:1i76, PDBj:1i76
PDBsum1i76
PubMed10978185
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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