Structure of PDB 5bpa Chain B

Receptor sequence

>5bpaB (length=166) Species: 9606 (Homo sapiens) [Search protein sequence]

YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPG

3D structure

PDB

5bpa Fragment-based discovery of indole inhibitors of matrix metalloproteinase-13.

Chain

Resolution

1.79 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	D128 D203 E205	D25 D100 E102
BS04	CA	B	D179 G180 S182 L184 D202 E205	D76 G77 S79 L81 D99 E102
BS05	CA	B	D162 N194 G196 D198	D59 N91 G93 D95
BS06	4UF	B	K140 F217 L218 H222 L239 F241 I243 Y244 Y246 T247 K249 S250 F252	K37 F114 L115 H119 L136 F138 I140 Y141 Y143 T144 K146 S147 F149	MOAD: ic50=0.001uM BindingDB: IC50=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

View graph for
Cellular Component

External links

PDB	RCSB:5bpa, PDBe:5bpa, PDBj:5bpa
PDBsum	5bpa
PubMed	22017539
UniProt	P45452\|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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