Structure of PDB 3kry Chain B

Receptor sequence

>3kryB (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]

YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYG

3D structure

PDB

3kry Orally-active MMP-1 sparing alpha-tetrahydropyranyl and alpha-piperidinyl sulfone matrix metalloproteinase (MMP) inhibitors with efficacy in cancer, arthritis, and cardiovascular disease

Chain

Resolution

1.9 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	H222 E223 H226 H232
Catalytic site (residue number reindexed from 1)	H119 E120 H123 H129
Enzyme Commision number	3.4.24.-

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	B	H172 D174 H187 H200	H69 D71 H84 H97
BS02	ZN	B	H222 H226 H232	H119 H123 H129
BS03	CA	B	D162 N194 Y195 G196 D198	D59 N91 Y92 G93 D95
BS04	CA	B	D179 G180 S182 L184 D202 E205	D76 G77 S79 L81 D99 E102
BS05	3KR	B	L184 L185 A186 H222 E223 H226 H232 L239 F241 P242 I243 T245	L81 L82 A83 H119 E120 H123 H129 L136 F138 P139 I140 T142	MOAD: ic50=0.1nM

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:3kry, PDBe:3kry, PDBj:3kry
PDBsum	3kry
PubMed	20726512
UniProt	P45452\|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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