Structure of PDB 3ow1 Chain H

Receptor sequence
>3ow1H (length=387) Species: 158080 () [Search protein sequence]
LKIRDAYTIVTCPGRNFVTLKIVTESGTHGIGDATLNGREMAVAAYLDEH
VVPALIGRDAGRIEDTWQYLYRGAYWRRGPVTMTAIAAVDMALWDIKAKA
AGMPLYQLLGGKSRERVMTYAHCTGQTIEDCLGEVARHVELGYRAVRVQS
GVPGPADSSLPAEHVWSTEKYLNHAPKLFAAVRERFGDDLHVLHDVHHRL
TPIEAARLGKAVEPYHLFWLEDCVPAENQESLRLIREHTTTPLAIGEVFN
SIHDCRELIQNQWIDYIRMPLTHGGGITAMRRVADLASLYHVRTGFHGPT
DLSPVCLGAAIHFDTWVPNFGIQEHMPHTDETDAVFPHDYRFEDGHFLAG
ESPGHGVDIDEELAAKYPYERASLPVNRLEDGTLWHW
3D structure
PDB3ow1 CRYSTAL STRUCTURE OF D-MANNONATE DEHYDRATASE FROM CHROMOHALOBACTER SALEXIGENS complexed with MG
ChainH
Resolution1.798 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 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 H 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

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Molecular Function
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Biological Process
External links
PDB RCSB:3ow1, PDBe:3ow1, PDBj:3ow1
PDBsum3ow1
PubMed
UniProtQ1QT89|DMGD_CHRSD D-galactonate dehydratase family member ManD (Gene Name=manD)

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