Structure of PDB 1a86 Chain A

Receptor sequence
>1a86A (length=158) Species: 9606 (Homo sapiens) [Search protein sequence]
NPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQG
EADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTN
TSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDI
DGIQAIYG
3D structure
PDB1a86 Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.
ChainA
Resolution2.0 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) H113 E114 H117 H123
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 0ZB A I159 L160 A161 H197 E198 H201 H207 L214 Y216 N218 Y219 I75 L76 A77 H113 E114 H117 H123 L130 Y132 N134 Y135 PDBbind-CN: -logKd/Ki=4.00,IC50=101uM
BindingDB: Ki=88000nM
BS02 CA A D137 G169 I170 G171 D173 D53 G85 I86 G87 D89
BS03 CA A D154 G155 N157 I159 D177 E180 D70 G71 N73 I75 D93 E96
BS04 ZN A H147 D149 H162 H175 H63 D65 H78 H91
BS05 ZN A H197 H201 H207 H113 H117 H123
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:1a86, PDBe:1a86, PDBj:1a86
PDBsum1a86
PubMed9655333
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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