Structure of PDB 2gge Chain C

Receptor sequence
>2ggeC (length=374) Species: 1423 (Bacillus subtilis) [Search protein sequence]
ALVKIVRIETFPLFHRLEKPYGDANGFKRYRTCYLIRIITESGIDGWGEC
VDWLPALHVGFTKRIIPFLLGKQAGSRLSLVRTIQKWHQRAASAVSMALT
EIAAKAADCSVCELWGGRYREEIPVYASFQSYSDSPQWISRSVSNVEAQL
KKGFEQIKVKIGGTSFKEDVRHINALQHTAGSSITMILDANQSYDAAAAF
KWERYFSEWTNIGWLEEPLPFDQPQDYAMLRSRLSVPVAGGENMKGPAQY
VPLLSQRCLDIIQPDVMHVNGIDEFRDCLQLARYFGVRASAHAYDGSLSR
LYALFAQACLPPWSKMKNDHIEPIEWDVMENPFTDLVSLQPSKGMVHIPK
GKGIGTEINMEIVNRYKWDGSAYE
3D structure
PDB2gge Crystal Structure of Mandelate Racemase/Muconate Lactonizing Enzyme from Bacillus Subtilis complexed with MG++ at 1.8 A
ChainC
Resolution1.89 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) Y21 S128 K158 K160 D189 N191 E216 G241 E242 D265 H292 N318 D319 E325
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 C E217 E243 H293 E216 E242 H292
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

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

[Back to BioLiP]