Structure of PDB 3gah Chain A

Receptor sequence
>3gahA (length=186) Species: 1598 (Limosilactobacillus reuteri) [Search protein sequence]
KIYTKNGDKGQTRIIGKQILYKNDPRVAAYGEVDELNSWVGYTKSLINSH
TQVLSNELEEIQQLLFDCGHDLATPADDERHSFKFKQEQPTVWLEEKIDN
YTQVVPAVKKHILPGGTQLASALHVARTITRRAERQIVQLMREEQINQDV
LIFINRLSDYFFAAARYANYLEQQPDMLYRNSKDVF
3D structure
PDB3gah Residue Phe112 of the human-type corrinoid adenosyltransferase (PduO) enzyme of Lactobacillus reuteri is critical to the formation of the four-coordinate Co(II) corrinoid substrate and to the activity of the enzyme.
ChainA
Resolution1.17 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
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 ATP A T5 K6 G8 T13 R14 K23 V28 Y31 T4 K5 G7 T12 R13 K22 V27 Y30
BS02 B12 A K2 D35 F67 G70 H71 K1 D34 F66 G69 H70
BS03 MG A P76 A77 D79 H82 P75 A76 D78 H81
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008817 corrinoid adenosyltransferase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0009236 cobalamin biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3gah, PDBe:3gah, PDBj:3gah
PDBsum3gah
PubMed19236001
UniProtQ50EJ2

[Back to BioLiP]