Structure of PDB 1g64 Chain A

Receptor sequence
>1g64A (length=169) [Search protein sequence]
RGIIIVFTGNGKGKTTAAFGTAARAVGHGKNVGVVQFIKGTWPNGERNLL
EPHGVEFQVMATGFTWETQNREADTAACMAVWQHGKRMLADPLLDMVVLD
ELTYMVAYDYLPLEEVISALNARPGHQTVIITGRGCHRDILDLADTVSEL
RPVKHAFDAGVKAQMGIDY
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.
ChainA
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) N37 K39 K41 T42 T43 R51 F91 W93 E128
Catalytic site (residue number reindexed from 1) N10 K12 K14 T15 T16 R24 F64 W66 E101
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 A T42 E128 T15 E101
BS02 B12 A W93 Y131 R161 W66 Y104 R134
BS03 ATP A K39 G40 K41 T42 T43 H182 D195 K12 G13 K14 T15 T16 H155 D168
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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Molecular Function
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Biological Process
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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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