Structure of PDB 3pk7 Chain D

Receptor sequence

>3pk7D (length=387) Species: 158080 ()

SLKIRDAYTIVTCPGRNFVTLKIVTESGTHGIGDATLNGREMAVAAYLDE
HVVPALIGRDAGRIEDTWQYLYRGAYWRRGPVTMTAIAAVDMALWDIKAK
AAGMPLYQLLGGKSRERVMTYAHCTGQTIEDCLGEVARHVELGYRAVRVQ
SGVPGIESSLPAEHVWSTEKYLNHAPKLFAAVRERFGDDLHVLHDVHHRL
TPIEAARLGKAVEPYHLFWLEDCVPAENQESLRLIREHTTTPLAIGEVFN
SIHDCRELIQNQWIDYIRMPLTHGGGITAMRRVADLASLYHVRTGFHGPT
DLSPVCLGAAIHFDTWVPNFGIQEHMPHTDETDAVFPHDYRFEDGHFLAG
ESPGHGVDIDEELAAKYPYERASLPVNRLEDGTLWHW

3D structure

• PDB: 3pk7 Crystal structure of D-mannonate dehydratase from Chromohalobacter salexigens with MG and Glycerol bound in the active site
• Chain: D
• 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): H123 R148 Q150 D195 H197 E221 G246 E247 R268 P270 H297 G298 E324 W387
• 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	D	D213 E239 E265	D195 E221 E247

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)