Structure of PDB 4k1w Chain A

Receptor sequence

>4k1wA (length=395) Species: 279238 (Novosphingobium aromaticivorans DSM 12444)

SSGLVPRGSHMKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRE
LSVVAYLQEHVAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVD
MALWDIKAKMAGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYID
MGYKAIRAQTGVPGIKSLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHL
LHDGHHRYTPQEAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTP
LAVGEIFNTIWDAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQV
RTGCHGPTDLSPVTMGCALHFDTWVPNFGIQEYMRHTEETDAVFPHDYWF
EKGELFVGETPGHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW

3D structure

• PDB: 4k1w Crystal structure of the A314P mutant of mannonate dehydratase from novosphingobium aromaticivorans complexed with mg and d-mannonate
• Chain: A
• Resolution: 1.646 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): G131 R157 Q159 D203 H205 E229 G254 E255 R276 T278 H305 E332 W395
• 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	D203 E229 E255
BS02	CS2	A	N37 D210 H212 E262 H312 P314 D316 E339 L389 W402	N47 D203 H205 E255 H305 P307 D309 E332 L382 W395
BS03	PDO	A	W181 H209 Y215	W174 H202 Y208

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:4k1w, PDBe:4k1w, PDBj:4k1w
• PDBsum: 4k1w
• UniProt: A4XF23|MAND_NOVAD D-mannonate dehydratase (Gene Name=manD)