Structure of PDB 4k2s Chain G

Receptor sequence
>4k2sG (length=392) Species: 290398 (Chromohalobacter israelensis DSM 3043) [Search protein sequence]
LKIRDAYTIVTCPGRNFVTLKIVTESGTHGIGDATLNGREMAVAAYLDEH
VVPALIGRDAGRIEDTWQYLYRGAYWRRGPVTMTAIAAVDMALWDIKAKA
AGMPLYQLLGGKSRERVMTYAHCTGQTIEDCLGEVARHVELGYRAVRVQS
GVPGIETTYGVDSSLPAEHVWSTEKYLNHAPKLFAAVRERFGDDLHVLHD
VHHRLTPIEAARLGKAVEPYHLFWLEDCVPAENQESLRLIREHTTTPLAI
GEVFNSIHDCRELIQNQWIDYIRMPLTHGGGITAMRRVADLASLYHVRTG
FHGATDLSPVCLGAAIHFDTWVPNFGIQEHMPHTDETDAVFPHDYRFEDG
HFLAGESPGHGVDIDEELAAKYPYERASLPVNRLEDGTLWHW
3D structure
PDB4k2s Crystal structure of the mutant P317A of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg and d-gluconate
ChainG
Resolution1.699 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 D200 H202 E226 G251 E252 R273 P275 H302 G303 E329 W392
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 A317 D319 E342 N37 Y159 D200 H202 E252 H302 A304 D306 E329
BS02 MG G D213 E239 E265 D200 E226 E252
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4k2s, PDBe:4k2s, PDBj:4k2s
PDBsum4k2s
PubMed
UniProtQ1QT89|DMGD_CHRSD D-galactonate dehydratase family member ManD (Gene Name=manD)

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