Structure of PDB 3o2x Chain B

Receptor sequence

>3o2xB (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]

ANVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYG

3D structure

PDB

3o2x MMP-13 in complex with selective tetrazole core inhibitor

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)	H2222 E2223 H2226 H2232
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	3O2	B	L2184 L2185 A2186 H2222 E2223 H2226 H2232 L2239 P2242 T2245 G2248 F2252 M2253	L81 L82 A83 H119 E120 H123 H129 L136 P139 T142 G145 F149 M150	BindingDB: Ki=0.130000nM
BS02	ZN	B	H2172 D2174 H2187 H2200	H69 D71 H84 H97
BS03	ZN	B	H2222 H2226 H2232	H119 H123 H129
BS04	CA	B	D2162 N2194 Y2195 G2196 D2198	D59 N91 Y92 G93 D95
BS05	CA	B	D2179 G2180 S2182 L2184 D2202 E2205	D76 G77 S79 L81 D99 E102

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

View graph for
Cellular Component

External links

PDB	RCSB:3o2x, PDBe:3o2x, PDBj:3o2x
PDBsum	3o2x
PubMed
UniProt	P45452\|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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