Structure of PDB 2qjj Chain C

Receptor sequence
>2qjjC (length=384) Species: 48935 (Novosphingobium aromaticivorans) [Search protein sequence]
MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEH
VAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKM
AGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQT
GVPGISLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTPQ
EAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTIW
DAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGATDLS
PVTMGCALHFDTWVPNFGIQEYMRHTEETDAVFPHDYWFEKGELFVGETP
GHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW
3D structure
PDB2qjj Evolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans.
ChainC
Resolution1.8 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 D192 H194 E218 G243 E244 R265 T267 H294 E321 W384
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 C D210 E236 E262 D192 E218 E244
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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