Structure of PDB 1c2t Chain B

Receptor sequence

>1c2tB (length=209) Species: 562 (Escherichia coli)

MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAG
IATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHY
AGRLLNIHPSLLPKYPGLHTHRQALENGDEEHGTSVHFVTDELDGGPVIL
QAKVPVFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDG
QRLPPQGYA

3D structure

• PDB: 1c2t New insights into inhibitor design from the crystal structure and NMR studies of Escherichia coli GAR transformylase in complex with beta-GAR and 10-formyl-5,8,10-trideazafolic acid.
• Chain: B
• Resolution: 2.1 Å

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	NHS	B	R64 F88 M89 R90 I91 L92 N106 H108 L118 V139 T140 D141 L143 D144	R64 F88 M89 R90 I91 L92 N106 H108 L118 V139 T140 D141 L143 D144	MOAD: Ki=260nM PDBbind-CN: -logKd/Ki=6.59,Ki=260nM
BS02	GAR	B	G11 S12 N13 G87 F88 M89 P109 E173	G11 S12 N13 G87 F88 M89 P109 E173

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

External links

• PDB: RCSB:1c2t, PDBe:1c2t, PDBj:1c2t
• PDBsum: 1c2t
• PubMed: 10606510
• UniProt: P08179|PUR3_ECOLI Phosphoribosylglycinamide formyltransferase (Gene Name=purN)