Structure of PDB 1jkx Chain A

Receptor sequence
>1jkxA (length=209) Species: 562 (Escherichia coli) [Search protein sequence]
MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAG
IATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHY
AGRLLNIHPSLLPKYPGLHTHRQALENGDEEHGTSVHFVTDELDGGPVIL
QAKVPVFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG
QRLPPQGYA
3D structure
PDB1jkx Unexpected formation of an epoxide-derived multisubstrate adduct inhibitor on the active site of GAR transformylase.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) N106 H108 S135 D144
Catalytic site (residue number reindexed from 1) N106 H108 S135 D144
Enzyme Commision number 2.1.2.2: phosphoribosylglycinamide formyltransferase 1.
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 138 A N10 G11 S12 N13 R64 G87 F88 M89 R90 I91 L92 I107 P109 Q170 E173 N10 G11 S12 N13 R64 G87 F88 M89 R90 I91 L92 I107 P109 Q170 E173 MOAD: Ki=20uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004644 phosphoribosylglycinamide formyltransferase activity
GO:0016740 transferase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0006974 DNA damage response
GO:0009058 biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1jkx, PDBe:1jkx, PDBj:1jkx
PDBsum1jkx
PubMed11695901
UniProtP08179|PUR3_ECOLI Phosphoribosylglycinamide formyltransferase (Gene Name=purN)

[Back to BioLiP]