Structure of PDB 4jqg Chain A

Receptor sequence

>4jqgA (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]

GFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLT
FTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFD
DDELWSLGKGVGYSLFLVAAHAFGHALGLDHSSVPEALMYPMYRFTEGPP
LHKDDVNGIRHLYG

3D structure

PDB

4jqg Halogen Bonding Controls Selectivity of FRET Substrate Probes for MMP-9.

Chain

Resolution

1.849 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	H226 H230 H236
Catalytic site (residue number reindexed from 1)	H121 H125 H131
Enzyme Commision number	3.4.24.35: gelatinase B.

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)
BS01	peptide	A	G106 Q108 T109 F110 Y179 G186 L187 L188 A189 H190 A191 F192 I198 Y218 H226 H230 H236 P246 M247 Y248	G1 Q3 T4 F5 Y74 G81 L82 L83 A84 H85 A86 F87 I93 Y113 H121 H125 H131 P141 M142 Y143
BS02	AZI	A	H190 H226 A227 H230	H85 H121 A122 H125
BS03	ZN	A	H226 H230 H236	H121 H125 H131
BS04	ZN	A	H175 D177 H190 H203	H70 D72 H85 H98
BS05	CA	A	D182 G183 D185 L187 D205 E208	D77 G78 D80 L82 D100 E103
BS06	CA	A	D131 D206 E208	D26 D101 E103

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:4jqg, PDBe:4jqg, PDBj:4jqg
PDBsum	4jqg
PubMed	24583051
UniProt	P14780\|MMP9_HUMAN Matrix metalloproteinase-9 (Gene Name=MMP9)

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