Structure of PDB 2jsd Chain A Binding Site BS01

Receptor Information
>2jsd Chain A (length=160) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GEPKWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINS
GEADIMISFENGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWT
MGTNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDD
VKGIQALYGP
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2jsd Chain A Residue 273 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2jsd Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.
ResolutionN/A
Binding residue
(original residue number in PDB)		D183 G184 R186 T188 D206 E209
Binding residue
(residue number reindexed from 1)		D71 G72 R74 T76 D94 E97
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H226 E227 H230 H236
Catalytic site (residue number reindexed from 1) H114 E115 H118 H124
Enzyme Commision number 3.4.24.-
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:2jsd, PDBe:2jsd, PDBj:2jsd
PDBsum2jsd
PubMed17869250
UniProtO60882|MMP20_HUMAN Matrix metalloproteinase-20 (Gene Name=MMP20)

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