Structure of PDB 3d6n Chain A Binding Site BS02

Receptor Information
>3d6n Chain A (length=422) Species: 63363 (Aquifex aeolicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILVPEAEIIDAKG
LIVCPGFIDIHVHLRDPGQTYKEDIESGSRCAVAGGFTTIVCMPNTNPPI
DNTTVVNYILQKSKSVGLCRVLPTGTITKGRKGKEIADFYSLKEAGCVAF
TDDGSPVMDSSVMRKALELASQLGVPIMDHCEDDKLAYGVINEGEVSALL
GLSSRAPEAEEIQIARDGILAQRTGGHVHIQHVSTKLSLEIIEFFKEKGV
KITCEVNPNHLLFTEREVLNSGANARVNPPLRKKEDRLALIEGVKRGIID
CFATDHAPHQTFEKELVEFAMPGIIGLQTALPSALELYRKGIISLKKLIE
MFTINPARIIGVDLGTLKLGSPADITIFDPNKEWILNEETNLSKSRNTPL
WGKVLKGKVIYTIKDGKMVYKD
Ligand information
Ligand IDFLC
InChIInChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12)/p-3
InChIKeyKRKNYBCHXYNGOX-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341OC(CC([O-])=O)(CC([O-])=O)C([O-])=O
OpenEye OEToolkits 1.5.0C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
ACDLabs 10.04O=C([O-])CC(O)(C([O-])=O)CC(=O)[O-]
FormulaC6 H5 O7
NameCITRATE ANION
ChEMBL
DrugBank
ZINC
PDB chain3d6n Chain A Residue 424 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3d6n Dihydroorotase from the hyperthermophile Aquifiex aeolicus is activated by stoichiometric association with aspartate transcarbamoylase and forms a one-pot reactor for pyrimidine biosynthesis.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		H63 R65 D153 G154 H180 V277 N278 D305 H309 P322 G323
Binding residue
(residue number reindexed from 1)		H63 R65 D153 G154 H180 V277 N278 D305 H309 P322 G323
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H61 H63
Catalytic site (residue number reindexed from 1) H61 H63
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:3d6n, PDBe:3d6n, PDBj:3d6n
PDBsum3d6n
PubMed19128030
UniProtO66990|PYRC_AQUAE Dihydroorotase (Gene Name=pyrC)

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