Structure of PDB 3qke Chain B Binding Site BS02

Receptor Information
>3qke Chain B (length=397) Species: 158080 () [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LKIRDAYTIVTCPGRNFVTLKIVTESGTHGIGDATLNGREMAVAAYLDEH
VVPALIGRDAGRIEDTWQYLYRGAYWRRGPVTMTAIAAVDMALWDIKAKA
AGMPLYQLLGGKSRERVMTYAHCTGQTIEDCLGEVARHVELGYRAVRVQS
GVPGIETTYGVAYEPADSSLPAEHVWSTEKYLNHAPKLFAAVRERFGDDL
HVLHDVHHRLTPIEAARLGKAVEPYHLFWLEDCVPAENQESLRLIREHTT
TPLAIGEVFNSIHDCRELIQNQWIDYIRMPLTHGGGITAMRRVADLASLY
HVRTGFHGPTDLSPVCLGAAIHFDTWVPNFGIQEHMPHTDETDAVFPHDY
RFEDGHFLAGESPGHGVDIDEELAAKYPYERASLPVNRLEDGTLWHW
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3qke Chain B Residue 407 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3qke Cystal structure of D-mannonate dehydratase from Chromohalobacter salexigens complexed with Mg and D-Gluconate
Resolution1.55 Å
Binding residue
(original residue number in PDB)		D213 E239 E265
Binding residue
(residue number reindexed from 1)		D205 E231 E257
Annotation score1
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.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3qke, PDBe:3qke, PDBj:3qke
PDBsum3qke
PubMed
UniProtQ1QT89|DMGD_CHRSD D-galactonate dehydratase family member ManD (Gene Name=manD)

[Back to BioLiP]