Structure of PDB 3tt4 Chain A

Receptor sequence
>3tt4A (length=159) Species: 9606 (Homo sapiens) [Search protein sequence]
GNPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQ
GEADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWT
NTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDD
IDGIQAIYG
3D structure
PDB3tt4 Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins.
ChainA
Resolution1.88 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) H114 E115 H118 H124
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 ZN A H147 D149 H162 H175 H64 D66 H79 H92
BS02 ZN A H197 H201 H207 H114 H118 H124
BS03 CA A D154 G155 N157 I159 D177 E180 D71 G72 N74 I76 D94 E97
BS04 CA A D137 G169 I170 G171 D173 D54 G86 I87 G88 D90
BS05 E1S A I159 L160 A161 H197 E198 H201 H207 L214 Y216 P217 N218 Y219 A220 R222 I76 L77 A78 H114 E115 H118 H124 L131 Y133 P134 N135 Y136 A137 R139 MOAD: Ki=5.3nM
PDBbind-CN: -logKd/Ki=8.28,Ki=5.3nM
BindingDB: Ki=5.3nM
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:3tt4, PDBe:3tt4, PDBj:3tt4
PDBsum3tt4
PubMed22689580
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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