Structure of PDB 2jt5 Chain A

Receptor sequence

>2jt5A (length=161) Species: 9606 (Homo sapiens)

GIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYE
GEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWT
KDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQD
DINGIQSLYGP

3D structure

• PDB: 2jt5 Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors
• Chain: A
• Resolution: N/A

Enzymatic activity

• Catalytic site (original residue number in PDB): H201 E202 H205 H211
• Catalytic site (residue number reindexed from 1): H114 E115 H118 H124
• Enzyme Commision number: 3.4.24.17: stromelysin 1.

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	H114 H118 H124
BS02	ZN	A	H151 D153 H166 H179	H64 D66 H79 H92
BS03	CA	A	D158 G159 P160 G161 V163 E184	D71 G72 P73 G74 V76 E97
BS04	CA	A	E139 D141 N175 D177	E52 D54 N88 D90
BS05	JT5	A	N162 V163 L164 A165 L197 H201 E202 H205 H211 L218 Y220 P221 L222 Y223	N75 V76 L77 A78 L110 H114 E115 H118 H124 L131 Y133 P134 L135 Y136	PDBbind-CN: -logKd/Ki=7.74,Ki=18nM

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:2jt5, PDBe:2jt5, PDBj:2jt5
• PDBsum: 2jt5
• PubMed: 17710450
• UniProt: P08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)