Structure of PDB 3qke Chain G

Receptor sequence

>3qkeG (length=397) Species: 158080 ()

LKIRDAYTIVTCPGRNFVTLKIVTESGTHGIGDATLNGREMAVAAYLDEH
VVPALIGRDAGRIEDTWQYLYRGAYWRRGPVTMTAIAAVDMALWDIKAKA
AGMPLYQLLGGKSRERVMTYAHCTGQTIEDCLGEVARHVELGYRAVRVQS
GVPGIETTYGVAYEPADSSLPAEHVWSTEKYLNHAPKLFAAVRERFGDDL
HVLHDVHHRLTPIEAARLGKAVEPYHLFWLEDCVPAENQESLRLIREHTT
TPLAIGEVFNSIHDCRELIQNQWIDYIRMPLTHGGGITAMRRVADLASLY
HVRTGFHGPTDLSPVCLGAAIHFDTWVPNFGIQEHMPHTDETDAVFPHDY
RFEDGHFLAGESPGHGVDIDEELAAKYPYERASLPVNRLEDGTLWHW

3D structure

• PDB: 3qke Cystal structure of D-mannonate dehydratase from Chromohalobacter salexigens complexed with Mg and D-Gluconate
• Chain: G
• Resolution: 1.55 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H124 R149 Q151 Y161 D213 H215 E239 G264 E265 R286 P288 H315 G316 E342 W405
• Catalytic site (residue number reindexed from 1): H122 R147 Q149 Y159 D205 H207 E231 G256 E257 R278 P280 H307 G308 E334 W397
• 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	GCO	G	N39 Y161 D213 H215 E265 H315 P317 D319 E342 W405	N37 Y159 D205 H207 E257 H307 P309 D311 E334 W397
BS02	MG	G	D213 E239 E265	D205 E231 E257

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