Structure of PDB 1cde Chain C

Receptor sequence
>1cdeC (length=209) Species: 562 (Escherichia coli) [Search protein sequence]
MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAG
IATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHY
AGRLLNIHPSLLPKYPGLHTHRQALENGDEEHGTSVHFVTDELDGGPVIL
QAKVPVFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG
QRLPPQGYA
3D structure
PDB1cde Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase.
ChainC
Resolution2.5 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 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 GAR C N10 G11 S12 N13 G87 P109 Q170 E173 N10 G11 S12 N13 G87 P109 Q170 E173
BS02 DZF C M89 R90 I91 L92 V139 T140 L143 D144 M89 R90 I91 L92 V139 T140 L143 D144
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1cde, PDBe:1cde, PDBj:1cde
PDBsum1cde
PubMed1631098
UniProtP08179|PUR3_ECOLI Phosphoribosylglycinamide formyltransferase (Gene Name=purN)

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