Structure of PDB 4a1o Chain B Binding Site BS04

Receptor Information
>4a1o Chain B (length=517) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RRPIRRALISVYDKTGLVDLAQGLSAAGVEIISTGSTAKTIADTGIPVTP
VEQLTGFPEVLDGRVKTLHPRVHAGLLADLRKSEHAAALEQLGIEAFELV
VVNLYPFSQTVESGASVDDCVEQIDIGGPAMVRAAAKNHPSAAVVTDPLG
YHGVLAALRAGGFTLAERKRLASLAFQHIAEYDIAVASWMQQTLAPEHPV
AAFPQWFGRSWRRVAMLRYGENPHQQAALYGDPTAWPGLAQAEQLHGKDM
SYNNFTDADAAWRAAFDHEQTCVAIIKHANPCGIAISSVSVADAHRKAHE
CDPLSAYGGVIAANTEVSVEMAEYVSTIFTEVIVAPGYAPGALDVLARKK
NIRVLVAAEPLAGGSELRPISGGLLIQQSDQLDAHGDNPANWTLATGSPA
DPATLTDLVFAWRACRAVKSNAIVIAADGATVGVGMGQVNRVDAARLAVE
RGGERVRGAVAASDAFFPFPDGLETLAAAGVTAVVHPGGSVRDEEVTEAA
AKAGVTLYLTGARHFAH
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain4a1o Chain B Residue 1526 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4a1o Structural Analyses of a Purine Biosynthetic Enzyme from Mycobacterium Tuberculosis Reveal a Novel Bound Nucleotide.
Resolution2.48 Å
Binding residue
(original residue number in PDB)		K20 T40 G41 S42 T43
Binding residue
(residue number reindexed from 1)		K14 T34 G35 S36 T37
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K283 H284 N427 H523
Catalytic site (residue number reindexed from 1) K277 H278 N421 H517
Enzyme Commision number 2.1.2.3: phosphoribosylaminoimidazolecarboxamide formyltransferase.
3.5.4.10: IMP cyclohydrolase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003937 IMP cyclohydrolase activity
GO:0004643 phosphoribosylaminoimidazolecarboxamide formyltransferase activity
GO:0016740 transferase activity
GO:0016787 hydrolase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
Cellular Component
GO:0005829 cytosol
GO:0005886 plasma membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4a1o, PDBe:4a1o, PDBj:4a1o
PDBsum4a1o
PubMed21956117
UniProtP9WHM7|PUR9_MYCTU Bifunctional purine biosynthesis protein PurH (Gene Name=purH)

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