Structure of PDB 3gy1 Chain A

Receptor sequence
>3gy1A (length=387) Species: 290402 (Clostridium beijerinckii NCIMB 8052) [Search protein sequence]
SLEPTIITDVLCYITKPDRHNLVVVKVETNKGIYGLGCATFQQRPKAVSL
VVSEYLKPILIGRDANNIEDLWQMMMVNSYWRNGPILNNAISGVDMALWD
IKGKLANMPLYQLFGGKSRDAIAAYTHAVADNLEDLYTEIDEIRKKGYQH
IRCQLGFGSYFDQDEYMRTTVSMFSSLREKYGYKFHILHDVHERLFPNQA
VQFAKDVEKYKPYFIEDILPPDQNEWLGQIRSQTSTPLATGELFNNPMEW
KSLIANRQVDFIRCHVSQIGGITPALKLGSLCAAFGVRIAWHTPSDITPI
GVAVNIHLNINLHNAAIQENIEINDNTRCVFSGIPEAKNGFFYPIESPGI
GVDIDENEIIKYPVEYRPHEWTQSRIPDGTIVTEGHH
3D structure
PDB3gy1 CRYSTAL STRUCTURE OF putative mandelate racemase/muconate lactonizing protein from Clostridium beijerinckii NCIMB 8052
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R153 Q155 D207 H209 E233 G258 E259 R280 H282 H309 E336
Catalytic site (residue number reindexed from 1) R152 Q154 D190 H192 E216 G241 E242 R263 H265 H292 E319
Enzyme Commision number ?
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 A D207 E233 E259 D190 E216 E242
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0046872 metal ion binding
Biological Process
GO:0009063 amino acid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3gy1, PDBe:3gy1, PDBj:3gy1
PDBsum3gy1
PubMed
UniProtA6M2W4|IMAND_CLOB8 D-galactonate dehydratase family member Cbei_4837 (Gene Name=Cbei_4837)

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