Structure of PDB 2qjj Chain D Binding Site BS01

Receptor Information
>2qjj Chain D (length=387) Species: 48935 (Novosphingobium aromaticivorans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEH
VAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKM
AGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQT
GVPGIKDASLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRY
TPQEAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFN
TIWDAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGAT
DLSPVTMGCALHFDTWVPNFGIQEYMRHTEETDAVFPHDYWFEKGELFVG
ETPGHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain2qjj Chain D Residue 1004 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2qjj Evolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		D210 E236 E262
Binding residue
(residue number reindexed from 1)		D195 E221 E247
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G121 R147 Q149 D210 H212 E236 G261 E262 R283 T285 H312 E339 W402
Catalytic site (residue number reindexed from 1) G121 R147 Q149 D195 H197 E221 G246 E247 R268 T270 H297 E324 W387
Enzyme Commision number 4.2.1.8: mannonate dehydratase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008927 mannonate dehydratase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0009063 amino acid catabolic process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qjj, PDBe:2qjj, PDBj:2qjj
PDBsum2qjj
PubMed17944491
UniProtA4XF23|MAND_NOVAD D-mannonate dehydratase (Gene Name=manD)

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