Structure of PDB 1gar Chain A

Receptor sequence
>1garA (length=204) Species: 562 (Escherichia coli) [Search protein sequence]
MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAG
IATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHY
AGRLLNIHPSLLPKYPGLHTHNGDEEHGTSVHFVTDELDGGPVILQAKVP
VFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDGQRLPP
QGYA
3D structure
PDB1gar Towards structure-based drug design: crystal structure of a multisubstrate adduct complex of glycinamide ribonucleotide transformylase at 1.96 A resolution.
ChainA
Resolution1.96 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N106 H108 S135 D144
Catalytic site (residue number reindexed from 1) N106 H108 S130 D139
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 U89 A N10 G11 S12 N13 R64 G87 M89 R90 I91 L92 N106 I107 H108 P109 L143 D144 E173 N10 G11 S12 N13 R64 G87 M89 R90 I91 L92 N106 I107 H108 P109 L138 D139 E168 MOAD: Ki=100pM
PDBbind-CN: -logKd/Ki=10.00,Ki=100pM
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

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Cellular Component
External links
PDB RCSB:1gar, PDBe:1gar, PDBj:1gar
PDBsum1gar
PubMed7776369
UniProtP08179|PUR3_ECOLI Phosphoribosylglycinamide formyltransferase (Gene Name=purN)

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