Structure of PDB 1kbc Chain A

Receptor sequence
>1kbcA (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]
FMLTPGNPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIF
TRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDA
EETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYS
LPQDDIDGIQAIYG
3D structure
PDB1kbc 1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile.
ChainA
Resolution1.8 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) H119 E120 H123 H129
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 D59 G91 G93 D95
BS02 CA A D154 G155 N157 I159 D177 E180 D76 G77 N79 I81 D99 E102
BS03 ZN A H147 D149 H162 H175 H69 D71 H84 H97
BS04 ZN A H197 H201 H207 H119 H123 H129
BS05 HLE A L160 A161 H197 E198 H201 H207 P217 L82 A83 H119 E120 H123 H129 P139
BS06 RIN A G158 N218 Y219 G80 N140 Y141
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:1kbc, PDBe:1kbc, PDBj:1kbc
PDBsum1kbc
PubMed9249047
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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