Structure of PDB 1rsd Chain A

Receptor sequence
>1rsdA (length=121) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
MQDTIFLKGMRFYGYHGALSAENEIGQIFKVDVTLKVDLSEAGRTDNVID
TVHYGEVFEEVKSIMEGKAVNLLEHLAERIANRINSQYNRVMETKVRITK
ENPPIPGHYDGVGIEIVRENK
3D structure
PDB1rsd Discovery of Potent Inhibitors of Dihydroneopterin Aldolase Using CrystaLEAD High-Throughput X-ray Crystallographic Screening and Structure-Directed Lead Optimization.
ChainA
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) E22 K100
Catalytic site (residue number reindexed from 1) E22 K100
Enzyme Commision number 4.1.2.25: dihydroneopterin aldolase.
5.1.99.8: 7,8-dihydroneopterin epimerase.
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 PSB A L72 E74 P104 P106 L72 E74 P104 P106 MOAD: ic50=0.3uM
PDBbind-CN: -logKd/Ki=6.52,IC50=0.30uM
Gene Ontology
Molecular Function
GO:0004150 dihydroneopterin aldolase activity
GO:0016829 lyase activity
GO:0016853 isomerase activity
Biological Process
GO:0006760 folic acid-containing compound metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1rsd, PDBe:1rsd, PDBj:1rsd
PDBsum1rsd
PubMed15027862
UniProtP56740|FOLB_STAAU Dihydroneopterin aldolase (Gene Name=folB)

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