Structure of PDB 1q3a Chain B

Receptor sequence

>1q3aB (length=160) Species: 9606 (Homo sapiens)

GMPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYE
GEADIMISFAVKEHGDNYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWT
EDASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQD
DVNGIQSLYG

3D structure

• PDB: 1q3a Crystal structure of the catalytic domain of human matrix metalloproteinase 10.
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H217 E218 H221 H227
• Catalytic site (residue number reindexed from 1): H114 E115 H118 H124
• 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	B	H217 H221 H227	H114 H118 H124
BS02	ZN	B	H167 D169 H182 H195	H64 D66 H79 H92
BS03	CA	B	D174 G175 G177 S179 D197 E200	D71 G72 G74 S76 D94 E97
BS04	CA	B	D157 G189 L190 Y191 D193	D54 G86 L87 Y88 D90
BS05	CA	B	D123 D198 E200	D20 D95 E97
BS06	NGH	B	S179 L180 A181 H217 E218 H221 H227 P237 Y239	S76 L77 A78 H114 E115 H118 H124 P134 Y136

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

External links

• PDB: RCSB:1q3a, PDBe:1q3a, PDBj:1q3a
• PDBsum: 1q3a
• PubMed: 15095982
• UniProt: P09238|MMP10_HUMAN Stromelysin-2 (Gene Name=MMP10)