Structure of PDB 2oel Chain A

Receptor sequence
>2oelA (length=412) Species: 1462 (Geobacillus kaustophilus) [Search protein sequence]
SAVMATYLLHDETDIRKKAEGIALGLTIGTWTDLPALEQEQLRKHKGEVV
AIEELGESERVNAYFGKRLKRAIVKIAYPTVNFSADLPALLVTTFGKLSL
DGEVRLLDLEFPDEWKRQFPGPRFGIDGIRDRVGVHNRPLLMSIFKGMIG
RDLAYLTSELKKQALGGVDLVKDDEILFDSELLPFEKRITEGKAALQEVY
EQTGKRTLYAVNLTGKTFALKDKAKRAAELGADVLLFNVFAYGLDVLQAL
REDEEIAVPIMAHPAFSGAVTPSEFYGVAPSLWLGKLLRLAGADFVLFPS
PYGSVALEREQALGIARALTDDQEPFARAFPVPSAGIHPGLVPLIIRDFG
LDTIVNAGGGIHGHPDGAIGGGRAFRAAIDAVLAGRPLRAAAAENEALQK
AIDRWGVVEVEA
3D structure
PDB2oel Mechanistic Diversity in the RuBisCO Superfamily: The "Enolase" in the Methionine Salvage Pathway in Geobacillus kaustophilus.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K147 K173 D174 D175 E176 H264 L298 S305
Catalytic site (residue number reindexed from 1) K146 K172 D173 D174 E175 H263 L297 S304
Enzyme Commision number 5.3.2.5: 2,3-diketo-5-methylthiopentyl-1-phosphate enolase.
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 CO3 A A336 G337 I338 A335 G336 I337
BS02 MG A K173 D175 E176 K172 D174 E175
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016853 isomerase activity
GO:0016984 ribulose-bisphosphate carboxylase activity
GO:0043715 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009086 methionine biosynthetic process
GO:0015977 carbon fixation
GO:0019509 L-methionine salvage from methylthioadenosine

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Molecular Function
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Biological Process
External links
PDB RCSB:2oel, PDBe:2oel, PDBj:2oel
PDBsum2oel
PubMed17352497
UniProtQ5L1E2|MTNW_GEOKA 2,3-diketo-5-methylthiopentyl-1-phosphate enolase (Gene Name=mtnW)

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