Structure of PDB 1qib Chain A

Receptor sequence
>1qibA (length=161) Species: 9606 (Homo sapiens) [Search protein sequence]
RKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHD
GEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWS
LGKGVGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDI
KGIQELYGASP
3D structure
PDB1qib X-ray structure of gelatinase A catalytic domain complexed with a hydroxamate inhibitor
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H201 E202 H205 H211
Catalytic site (residue number reindexed from 1) H115 E116 H119 H125
Enzyme Commision number 3.4.24.24: gelatinase A.
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 A H201 H205 H211 H115 H119 H125
BS02 ZN A H151 D153 H166 H179 H64 D66 H79 H92
BS03 CA A D158 G159 D161 L163 D181 E184 D71 G72 D74 L76 D94 E97
BS04 CA A D141 G173 G175 D177 D54 G86 G88 D90
BS05 CA A D107 D182 E184 D20 D95 E97
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
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Cellular Component
External links
PDB RCSB:1qib, PDBe:1qib, PDBj:1qib
PDBsum1qib
PubMed
UniProtP08253|MMP2_HUMAN 72 kDa type IV collagenase (Gene Name=MMP2)

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