Structure of PDB 4hut Chain B

Receptor sequence

>4hutB (length=169) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2)

RGIIIVFTGNGKGKTTAAFGTAARAVGHGKNVGVVQFIKGTWPNGERNLL
EPHGVEFQVMATGFTWETQNREADTAACMAVWQHGKRMLADPLLDMVVLD
ELTYMVAYDYLPLEEVISALNARPGHQTVIITGRGCHRDILDLADTVSEL
RPVKHAFDAGVKAQMGIDY

3D structure

• PDB: 4hut Structural Insights into the Mechanism of Four-Coordinate Cob(II)alamin Formation in the Active Site of the Salmonella enterica ATP:Co(I)rrinoid Adenosyltransferase Enzyme: Critical Role of Residues Phe91 and Trp93.
• Chain: B
• Resolution: 1.95 Å

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	B	T42 E128	T15 E101
BS02	ATP	B	N37 K39 G40 K41 T42 T43 E128 H182 F184 D195	N10 K12 G13 K14 T15 T16 E101 H155 F157 D168
BS03	B12	B	I65 K66 T68 W69 G90 F91 T92 W93 E128 Y131 R161 F184 D195 Y196	I38 K39 T41 W42 G63 F64 T65 W66 E101 Y104 R134 F157 D168 Y169

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

External links

• PDB: RCSB:4hut, PDBe:4hut, PDBj:4hut
• PDBsum: 4hut
• PubMed: 23148601
• UniProt: P31570|BTUR_SALTY Corrinoid adenosyltransferase CobA (Gene Name=btuR)