Structure of PDB 2gge Chain A

Receptor sequence
>2ggeA (length=373) Species: 1423 (Bacillus subtilis) [Search protein sequence]
LVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIITESGIDGWGECV
DWLPALHVGFTKRIIPFLLGKQAGSRLSLVRTIQKWHQRAASAVSMALTE
IAAKAADCSVCELWGGRYREEIPVYASFQSYSDSPQWISRSVSNVEAQLK
KGFEQIKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAFK
WERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAGGENMKGPAQYV
PLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAYDGSLSRL
YALFAQACLPPWSKMKNDHIEPIEWDVMENPFTDLVSLQPSKGMVHIPKG
KGIGTEINMEIVNRYKWDGSAYE
3D structure
PDB2gge Crystal Structure of Mandelate Racemase/Muconate Lactonizing Enzyme from Bacillus Subtilis complexed with MG++ at 1.8 A
ChainA
Resolution1.89 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y22 S129 K159 K161 D190 N192 E217 G242 E243 D266 H293 N319 D320 E326
Catalytic site (residue number reindexed from 1) Y20 S127 K157 K159 D188 N190 E215 G240 E241 D264 H291 N317 D318 E324
Enzyme Commision number 5.-.-.-
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 E217 E243 H293 E215 E241 H291
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2gge, PDBe:2gge, PDBj:2gge
PDBsum2gge
PubMed
UniProtO06741|YITF_BACSU Putative isomerase YitF (Gene Name=yitF)

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