Structure of PDB 1kbc Chain B

Receptor sequence

>1kbcB (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]

FMLTPGNPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIF
TRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDA
EETWTNTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYS
LPQDDIDGIQAIYG

3D structure

PDB

1kbc 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.

Chain

Resolution

1.8 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)
BS01	CA	B	D137 G169 G171 D173	D59 G91 G93 D95
BS02	CA	B	D154 G155 N157 I159 D177 E180	D76 G77 N79 I81 D99 E102
BS03	ZN	B	H147 D149 H162 H175	H69 D71 H84 H97
BS04	ZN	B	H197 H201 H207	H119 H123 H129
BS05	HLE	B	I159 L160 A161 H197 E198 H201 H207 P217	I81 L82 A83 H119 E120 H123 H129 P139
BS06	RIN	B	G158 L160 N218 Y219	G80 L82 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
PDBsum	1kbc
PubMed	9249047
UniProt	P22894\|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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