Structure of PDB 3bul Chain A

Receptor sequence
>3bulA (length=577) Species: 562 (Escherichia coli) [Search protein sequence]
QAEWRSWEVNKRLEYSLVKGITEFIEQDTEEARQQATRPCEVIEGPLMDG
MNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASKEQCKTNGKMV
IATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADL
IGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNY
SGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVRIQHGRKKPR
TPPVTLEAARDNDFAFDWQAYTPPVAHRLGVQEVEASIETLRNYIDWTPF
FMTWSLAGKYPRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVG
LFPANRVGDDIEIYRDETRTHVINVSHHLRQQTEKTGFANYCLADFVAPK
LSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFA
EYLHERVRKVYWGYAPNENLSNEELIRENYQGIRPAPGYPACPEHTEKAT
IWELLEVEKHTGMKLTESFAMWPGASVSGWYFSHPDSKYYAVAQIQRDQV
EDYARRKGMSVTEVERWLAPNLGYDAD
3D structure
PDB3bul A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D757 H759 S810
Catalytic site (residue number reindexed from 1) D107 H109 S160
Enzyme Commision number 2.1.1.13: methionine synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0008705 methionine synthase activity
GO:0031419 cobalamin binding
GO:0046872 metal ion binding
Biological Process
GO:0009086 methionine biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:3bul, PDBe:3bul, PDBj:3bul
PDBsum3bul
PubMed18332423
UniProtP13009|METH_ECOLI Methionine synthase (Gene Name=metH)

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