Structure of PDB 1q3a Chain A

Receptor sequence
>1q3aA (length=156) Species: 9606 (Homo sapiens) [Search protein sequence]
MPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEG
EADIMISFAVKEHGDNYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWTE
DASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSLAQFRLSQDDVNG
IQSLYG
3D structure
PDB1q3a Crystal structure of the catalytic domain of human matrix metalloproteinase 10.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H217 E218 H221 H227
Catalytic site (residue number reindexed from 1) H113 E114 H117 H123
Enzyme Commision number 3.4.24.22: stromelysin 2.
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 H217 H221 H227 H113 H117 H123
BS02 ZN A H167 D169 H182 H195 H63 D65 H78 H91
BS03 CA A D174 G175 G177 S179 D197 E200 D70 G71 G73 S75 D93 E96
BS04 CA A D157 G189 Y191 D193 D53 G85 Y87 D89
BS05 CA A D123 D198 E200 D19 D94 E96
BS06 NGH A S179 L180 A181 H217 E218 H227 P237 S241 S75 L76 A77 H113 E114 H123 P133 S137
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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Cellular Component
External links
PDB RCSB:1q3a, PDBe:1q3a, PDBj:1q3a
PDBsum1q3a
PubMed15095982
UniProtP09238|MMP10_HUMAN Stromelysin-2 (Gene Name=MMP10)

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