Structure of PDB 2qjn Chain A

Receptor sequence
>2qjnA (length=385) Species: 48935 (Novosphingobium aromaticivorans) [Search protein sequence]
MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEH
VAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKM
AGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQT
GVPGIASLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTP
QEAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTI
WDAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGATDL
SPVTMGCALHFDTWVPNFGIQEYMRHTEETDAVFPHDYWFEKGELFVGET
PGHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW
3D structure
PDB2qjn Evolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 MG A D210 E236 E262 D193 E219 E245
BS02 KDG A N37 D210 H212 E262 H312 A314 D316 E339 L389 W402 N37 D193 H195 E245 H295 A297 D299 E322 L372 W385
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
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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