Structure of PDB 2jnp Chain A

Receptor sequence
>2jnpA (length=161) Species: 9606 (Homo sapiens) [Search protein sequence]
GIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYE
GEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWT
KDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQD
DINGIQSLYGP
3D structure
PDB2jnp Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors
ChainA
ResolutionN/A
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) 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 H151 D153 H166 H179 H64 D66 H79 H92
BS02 ZN A H201 H205 H211 H114 H118 H124
BS03 CA A D158 G159 G161 V163 L164 D181 E184 D71 G72 G74 V76 L77 D94 E97
BS04 CA A D141 G173 N175 G176 D177 D54 G86 N88 G89 D90
BS05 NGH A L164 A165 H166 H201 E202 H205 H211 L77 A78 H79 H114 E115 H118 H124 PDBbind-CN: -logKd/Ki=6.89,Ki=130nM
BindingDB: Ki=132nM,IC50=6500nM
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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Biological Process
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Cellular Component
External links
PDB RCSB:2jnp, PDBe:2jnp, PDBj:2jnp
PDBsum2jnp
PubMed17710450
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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