Structure of PDB 4kpl Chain D

Receptor sequence
>4kplD (length=384) Species: 290398 (Chromohalobacter israelensis DSM 3043) [Search protein sequence]
LKIRDAYTIVTCPGRNFVTLKIVTESGTHGIGDATLNGREMAVAAYLDEH
VVPALIGRDAGRIEDTWQYLYRGAYWRRGPVTMTAIAAVDMALWDIKAKA
AGMPLYQLLGGKSRERVMTYAHCTGQTIEDCLGEVARHVELGYRAVRVQS
GVPGSSLPAEHVWSTEKYLNHAPKLFAAVRERFGDDLHVLHDVHHRLTPI
EAARLGKAVEPYHLFWLEDCVPAENQESLRLIREHTTTPLAIGEVFNSIH
DCRELIQNQWIDYIRMPLTHGGGITAMRRVADLASLYHVRTGFHGPTDLS
PVCLGAAIHFDTWVPNFGIQEHMPHTDETDAVFPHDYRFEDGHFLAGESP
GHGVDIDEELAAKYPYERASLPVNRLEDGTLWHW
3D structure
PDB4kpl Crystal structure of d-mannonate dehydratase from chromohalobacter salexigens complexed with Mg,d-mannonate and 2-keto-3-deoxy-d-gluconate
ChainD
Resolution2.0 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 D213 H215 E239 G264 E265 R286 P288 H315 G316 E342 W405
Catalytic site (residue number reindexed from 1) H122 R147 Q149 D192 H194 E218 G243 E244 R265 P267 H294 G295 E321 W384
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 KDG D N39 D213 H215 E265 H315 P317 D319 E342 N37 D192 H194 E244 H294 P296 D298 E321
BS02 MG D D213 E239 E265 D192 E218 E244
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:4kpl, PDBe:4kpl, PDBj:4kpl
PDBsum4kpl
PubMed
UniProtQ1QT89|DMGD_CHRSD D-galactonate dehydratase family member ManD (Gene Name=manD)

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