Structure of PDB 1g64 Chain B

Receptor sequence
>1g64B (length=190) [Search protein sequence]
QQRQQKVKDRVDARVAQAQEERGIIIVFTGNGKGKTTAAFGTAARAVGHG
KNVGVVQFIKGTWPNGERNLLEPHGVEFQVMATGFTWETQNREADTAACM
AVWQHGKRMLADPLLDMVVLDELTYMVAYDYLPLEEVISALNARPGHQTV
IITGRGCHRDILDLADTVSELRPVKHAFDAGVKAQMGIDY
3D structure
PDB1g64 Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N237 K239 K241 T242 T243 F291 W293 E328
Catalytic site (residue number reindexed from 1) N31 K33 K35 T36 T37 F85 W87 E122
Enzyme Commision number 2.5.1.17: corrinoid adenosyltransferase.
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 B T242 E328 T36 E122
BS02 ATP B K239 G240 K241 T242 T243 E328 H382 D395 K33 G34 K35 T36 T37 E122 H176 D189
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008817 corrinoid adenosyltransferase activity
GO:0016740 transferase activity
Biological Process
GO:0006779 porphyrin-containing compound biosynthetic process
GO:0009236 cobalamin biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1g64, PDBe:1g64, PDBj:1g64
PDBsum1g64
PubMed11148030
UniProtP31570|BTUR_SALTY Corrinoid adenosyltransferase CobA (Gene Name=btuR)

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