Structure of PDB 4yiw Chain A Binding Site BS02

Receptor Information
>4yiw Chain A (length=424) Species: 1392 (Bacillus anthracis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NYLFKNGRYMNEEGKIVATDLLVQDGKIAKVAENITADNAEVIDVNGKLI
APGLVDVHVHLREPGGEHKETIETGTLAAAKGGFTTICAMPNTRPVPDCR
EHMEDLQNRIKEKAHVNVLPYGAITVRQAGSEMTDFETLKELGAFAFTDD
GVGVQDASMMLAAMKRAAKLNMAVVAHCEENTLINKGCVHEGKFSEKHGL
NGIPSVCESVHIARDILLAEAADCHYHVCHVSTKGSVRVIRDAKRAGIKV
TAEVTPHHLVLCEDDIPSADPNFKMNPPLRGKEDHEALIEGLLDGTIDMI
ATDHAPHTAEEKAQGIERAPFGITGFETAFPLLYTNLVKKGIITLEQLIQ
FLTEKPADTFGLEAGRLKEGRTADITIIDLEQEEEIDPTTFLSKGKNTPF
AGWKCQGWPVMTIVGGKIAWQKES
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4yiw Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4yiw Ca-asp bound X-ray structure and inhibition of Bacillus anthracis dihydroorotase (DHOase).
Resolution2.45 Å
Binding residue
(original residue number in PDB)		D151 H178 H231
Binding residue
(residue number reindexed from 1)		D150 H177 H230
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H59 H61
Catalytic site (residue number reindexed from 1) H58 H60
Enzyme Commision number 3.5.2.3: dihydroorotase.
Gene Ontology
Molecular Function
GO:0004038 allantoinase activity
GO:0004151 dihydroorotase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
GO:0046872 metal ion binding
Biological Process
GO:0006145 purine nucleobase catabolic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0044205 'de novo' UMP 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:4yiw, PDBe:4yiw, PDBj:4yiw
PDBsum4yiw
PubMed27499369
UniProtQ81WF0|PYRC_BACAN Dihydroorotase (Gene Name=pyrC)

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