Structure of PDB 3dpf Chain A

Receptor sequence
>3dpfA (length=163) Species: 9606 (Homo sapiens) [Search protein sequence]
MLTPGNPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFT
RISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAE
ETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSL
PQDDIDGIQAIYG
3D structure
PDB3dpf Extra Binding Region Induced by Non-Zinc Chelating Inhibitors into the S(1)' Subsite of Matrix Metalloproteinase 8 (MMP-8)
ChainA
Resolution2.1 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 AXB A I159 L160 A161 L193 H197 L214 Y216 P217 N218 Y219 A220 R222 T224 Y227 S228 P230 I80 L81 A82 L114 H118 L135 Y137 P138 N139 Y140 A141 R143 T145 Y148 S149 P151 PDBbind-CN: -logKd/Ki=7.24,IC50=57nM
BindingDB: IC50=57nM
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:3dpf, PDBe:3dpf, PDBj:3dpf
PDBsum3dpf
PubMed19173605
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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