Structure of PDB 3pk7 Chain A

Receptor sequence

>3pk7A (length=396) Species: 158080 ()

LKIRDAYTIVTCPGRNFVTLKIVTESGTHGIGDATLNGREMAVAAYLDEH
VVPALIGRDAGRIEDTWQYLYRGAYWRRGPVTMTAIAAVDMALWDIKAKA
AGMPLYQLLGGKSRERVMTYAHCTGQTIEDCLGEVARHVELGYRAVRVQS
GVPGIETTYGVYEPADSSLPAEHVWSTEKYLNHAPKLFAAVRERFGDDLH
VLHDVHHRLTPIEAARLGKAVEPYHLFWLEDCVPAENQESLRLIREHTTT
PLAIGEVFNSIHDCRELIQNQWIDYIRMPLTHGGGITAMRRVADLASLYH
VRTGFHGPTDLSPVCLGAAIHFDTWVPNFGIQEHMPHTDETDAVFPHDYR
FEDGHFLAGESPGHGVDIDEELAAKYPYERASLPVNRLEDGTLWHW

3D structure

• PDB: 3pk7 Crystal structure of D-mannonate dehydratase from Chromohalobacter salexigens with MG and Glycerol bound in the active site
• Chain: A
• Resolution: 1.642 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H124 R149 Q151 D213 H215 E239 G264 E265 R286 P288 H315 G316 E342 W405
• Catalytic site (residue number reindexed from 1): H122 R147 Q149 D204 H206 E230 G255 E256 R277 P279 H306 G307 E333 W396
• Enzyme Commision number: 4.2.1.-
  4.2.1.39: gluconate dehydratase.
  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	D213 E239 E265	D204 E230 E256

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0008927 mannonate dehydratase activity
• GO:0016829 lyase activity
• GO:0046872 metal ion binding
• GO:0047929 gluconate dehydratase activity

Biological Process

• GO:0009063 amino acid catabolic process
• GO:0016052 carbohydrate catabolic process

External links

• PDB: RCSB:3pk7, PDBe:3pk7, PDBj:3pk7
• PDBsum: 3pk7
• UniProt: Q1QT89|DMGD_CHRSD D-galactonate dehydratase family member ManD (Gene Name=manD)