Structure of PDB 2ywr Chain A

Receptor sequence
>2ywrA (length=216) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
MLKIGVLVSGRGSNLQAIIDAIESGKVNASIELVISDNPKAYAIERCKKH
NVECKVIQRKEFPSKKEFEERMALELKKKGVELVVLAGFMRILSHNFLKY
FPNKVINIHPSLIPAFQGLHAQKQAVEFGVKFSGCTVHIVDESVDAGPVI
VQAVVPVLPEDDENTLADRILKWEHKILPQTVQWFAQDRIIIDGRKVIVK
DATYGTLPVNPALEIF
3D structure
PDB2ywr Structures and reaction mechanisms of the two related enzymes, PurN and PurU.
ChainA
Resolution1.77 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N107 H109 T136 D145
Catalytic site (residue number reindexed from 1) N107 H109 T136 D145
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 CO A H109 D145 H109 D145
BS02 CO A K131 V157 L158 P159 K131 V157 L158 P159
BS03 CO A I44 K48 C54 I44 K48 C54
Gene Ontology
Molecular Function
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:0009058 biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2ywr, PDBe:2ywr, PDBj:2ywr
PDBsum2ywr
PubMed24108189
UniProtO67023

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