Structure of PDB 1jap Chain A

Receptor sequence
>1japA (length=157) Species: 9606 (Homo sapiens) [Search protein sequence]
PKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGE
ADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTNT
SANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDID
GIQAIYG
3D structure
PDB1jap The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.
ChainA
Resolution1.82 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) H112 E113 H116 H122
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 peptide A S151 A161 H162 A163 F164 H201 H207 S66 A76 H77 A78 F79 H116 H122
BS02 CA A D137 G169 G171 D173 H197 E198 H201 D52 G84 G86 D88 H112 E113 H116
BS03 CA A D154 G155 N157 I159 D177 E180 D69 G70 N72 I74 D92 E95
BS04 ZN A H147 D149 H162 H175 H62 D64 H77 H90
BS05 ZN A H197 H201 H207 H112 H116 H122
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:1jap, PDBe:1jap, PDBj:1jap
PDBsum1jap
PubMed8137810
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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