Structure of PDB 2qjn Chain C

Receptor sequence

>2qjnC (length=384) Species: 48935 (Novosphingobium aromaticivorans)

MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEH
VAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKM
AGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQT
GVPGISLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTPQ
EAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTIW
DAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGATDLS
PVTMGCALHFDTWVPNFGIQEYMRHTEETDAVFPHDYWFEKGELFVGETP
GHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW

3D structure

• PDB: 2qjn Evolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans.
• Chain: C
• Resolution: 2.0 Å

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
BS02	KDG	C	N37 D210 H212 E262 H312 D316 E339 W402	N37 D192 H194 E244 H294 D298 E321 W384

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

External links

• PDB: RCSB:2qjn, PDBe:2qjn, PDBj:2qjn
• PDBsum: 2qjn
• PubMed: 17944491
• UniProt: A4XF23|MAND_NOVAD D-mannonate dehydratase (Gene Name=manD)