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Structure of PDB 1gar Chain B

Receptor sequence >1garB (length=193) Species: 562 (Escherichia coli) [Search protein sequence] MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAG IATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHY AGRLLNIHPSLLDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEDDIT ARVQTQEHAIYPLVISWFADGRLKMHENAAWLDGQRLPPQGYA

3D structure PDB 1gar Towards structure-based drug design: crystal structure of a multisubstrate adduct complex of glycinamide ribonucleotide transformylase at 1.96 A resolution. Chain B Resolution 1.96 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 S119 D128 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 B N10 G11 S12 N13 R64 G87 M89 R90 I91 L92 N106 H108 P109 V139 N10 G11 S12 N13 R64 G87 M89 R90 I91 L92 N106 H108 P109 V123 MOAD: 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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