Structure of PDB 3ljz Chain C

Receptor sequence

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

ANVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYG

3D structure

PDB

3ljz Structure analysis reveals the flexibility of the ADAMTS-5 active site.

Chain

Resolution

2.0 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	CA	C	D162 N194 D198	D59 N91 D95
BS02	CA	C	D179 G180 S182 L184 D202 E205	D76 G77 S79 L81 D99 E102
BS03	ZN	C	H172 D174 H187 H200	H69 D71 H84 H97
BS04	ZN	C	H222 H226 H232	H119 H123 H129
BS05	LA3	C	L184 L185 A186 L218 H222 E223 H226 H232 L239 F241 P242 I243 Y244 T245	L81 L82 A83 L115 H119 E120 H123 H129 L136 F138 P139 I140 Y141 T142	MOAD: Ki=7.3nM

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

View graph for
Molecular Function

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Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:3ljz, PDBe:3ljz, PDBj:3ljz
PDBsum	3ljz
PubMed	21370305
UniProt	P45452\|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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