Structure of PDB 3ljz Chain B

Receptor sequence

>3ljzB (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
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

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	B	D162 N194 Y195 D198	D59 N91 Y92 D95
BS02	CA	B	D179 G180 S182 L184 D202 E205	D76 G77 S79 L81 D99 E102
BS03	ZN	B	H172 D174 H187 H200	H69 D71 H84 H97
BS04	ZN	B	H222 H226 H232	H119 H123 H129
BS05	LA3	B	G183 L184 L185 A186 L218 H222 E223 H226 H232 L239 F241 P242 I243 Y244 T245	G80 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

View graph for
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)

[Back to BioLiP]