Structure of PDB 5v7y Chain A Binding Site BS02

Receptor Information
>5v7y Chain A (length=207) Species: 1392 (Bacillus anthracis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NKEQTIFDHKGNVIKTEDREIQIISKFEEPLIVVLGNVLSDEECDELIEL
SKSKLARSKVGSSRDVNDIRTSSGAFLDDNELTAKIEKRISSIMNVPASH
GEGLHILNYEVDQQYKAHYDYFAEHSRSAANNRISTLVMYLNDVEEGGET
FFPKLNLSVHPRKGMAVYFEYFYQDQSLNELTLHGGAPVTKGEKWIATQW
VRRGTYK
Ligand information
Ligand IDTFA
InChIInChI=1S/C2HF3O2/c3-2(4,5)1(6)7/h(H,6,7)
InChIKeyDTQVDTLACAAQTR-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01FC(F)(F)C(=O)O
CACTVS 3.370OC(=O)C(F)(F)F
OpenEye OEToolkits 1.7.0C(=O)(C(F)(F)F)O
FormulaC2 H F3 O2
Nametrifluoroacetic acid
ChEMBLCHEMBL506259
DrugBank
ZINCZINC000003860798
PDB chain5v7y Chain A Residue 303 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5v7y Bacillus anthracis Prolyl 4-Hydroxylase Interacts with and Modifies Elongation Factor Tu.
Resolution2.05 Å
Binding residue
(original residue number in PDB)		Y118 Y124 T159 G194 G195 K203
Binding residue
(residue number reindexed from 1)		Y109 Y115 T150 G185 G186 K194
Annotation score1
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

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:5v7y, PDBe:5v7y, PDBj:5v7y
PDBsum5v7y
PubMed28981257
UniProtA0A4Y1WAP5

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