Structure of PDB 2qjn Chain A Binding Site BS02

Receptor Information
>2qjn Chain A (length=385) Species: 48935 (Novosphingobium aromaticivorans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEH
VAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKM
AGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQT
GVPGIASLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTP
QEAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTI
WDAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGATDL
SPVTMGCALHFDTWVPNFGIQEYMRHTEETDAVFPHDYWFEKGELFVGET
PGHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW
Ligand information
Ligand IDKDG
InChIInChI=1S/C6H10O6/c7-2-5(10)3(8)1-4(9)6(11)12/h3,5,7-8,10H,1-2H2,(H,11,12)/t3-,5+/m0/s1
InChIKeyWPAMZTWLKIDIOP-WVZVXSGGSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C([C@@H]([C@@H](CO)O)O)C(=O)C(=O)O
CACTVS 3.341OC[C@@H](O)[C@@H](O)CC(=O)C(O)=O
ACDLabs 10.04O=C(C(=O)O)CC(O)C(O)CO
CACTVS 3.341OC[CH](O)[CH](O)CC(=O)C(O)=O
OpenEye OEToolkits 1.5.0C(C(C(CO)O)O)C(=O)C(=O)O
FormulaC6 H10 O6
Name2-KETO-3-DEOXYGLUCONATE
ChEMBL
DrugBank
ZINCZINC000001532568
PDB chain2qjn Chain A Residue 2001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2qjn Evolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		N37 D210 H212 E262 H312 A314 D316 E339 L389 W402
Binding residue
(residue number reindexed from 1)		N37 D193 H195 E245 H295 A297 D299 E322 L372 W385
Annotation score5
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 D193 H195 E219 G244 E245 R266 T268 H295 E322 W385
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2qjn, PDBe:2qjn, PDBj:2qjn
PDBsum2qjn
PubMed17944491
UniProtA4XF23|MAND_NOVAD D-mannonate dehydratase (Gene Name=manD)

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