Structure of PDB 5iax Chain A Binding Site BS02

Receptor Information
>5iax Chain A (length=199) Species: 1392 (Bacillus anthracis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EQTIFDHKGNVIKTEDREIQIISKFEEPLIVVLGNVLSDEECDELIELSK
SKLARSKVDVNDIAFLDDNELTAKIEKRISSIMNVPASHGEGLHILNYEV
DQQYKAHYDYFAEHSRSAANNRISTLVMYLNDVEEGGETFFPKLNLSVHP
RKGMAVYFEYFYQDQSLNELTLHGGAPVTKGEKWIATQWVRRGTYKPPG
Ligand information
Ligand IDAKG
InChIInChI=1S/C5H6O5/c6-3(5(9)10)1-2-4(7)8/h1-2H2,(H,7,8)(H,9,10)
InChIKeyKPGXRSRHYNQIFN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C(=O)CCC(=O)O
OpenEye OEToolkits 1.7.6C(CC(=O)O)C(=O)C(=O)O
CACTVS 3.385OC(=O)CCC(=O)C(O)=O
FormulaC5 H6 O5
Name2-OXOGLUTARIC ACID
ChEMBLCHEMBL1686
DrugBankDB08845
ZINCZINC000001532519
PDB chain5iax Chain A Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5iax Bacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		Y118 Y124 H127 D129 T159 H193 K203 I205 T207 W209
Binding residue
(residue number reindexed from 1)		Y98 Y104 H107 D109 T139 H173 K183 I185 T187 W189
Annotation score5
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0003674 molecular_function
GO:0004656 procollagen-proline 4-dioxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0031418 L-ascorbic acid binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0008150 biological_process
GO:0018401 peptidyl-proline hydroxylation to 4-hydroxy-L-proline

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5iax, PDBe:5iax, PDBj:5iax
PDBsum5iax
PubMed27129244
UniProtA0A4Y1WAP5

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