Structure of PDB 1xud Chain B

Receptor sequence

>1xudB (length=166) Species: 9606 (Homo sapiens) [Search protein sequence]

YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPG

3D structure

PDB

1xud Structural basis for the highly selective inhibition of MMP-13.

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)	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	H222 H226 H232	H119 H123 H129
BS02	ZN	B	H172 D174 H187 H200	H69 D71 H84 H97
BS03	CA	B	D179 G180 S182 L184 D202 E205	D76 G77 S79 L81 D99 E102
BS04	CA	B	D162 N194 Y195 G196 D198	D59 N91 Y92 G93 D95
BS05	PB4	B	F217 L218 V219 H222 L239 F241 I243 Y244 T245 Y246 T247 K249 S250 H251 F252	F114 L115 V116 H119 L136 F138 I140 Y141 T142 Y143 T144 K146 S147 H148 F149	MOAD: ic50=8nM BindingDB: IC50=8nM

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:1xud, PDBe:1xud, PDBj:1xud
PDBsum	1xud
PubMed	15734640
UniProt	P45452\|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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