Structure of PDB 4nhm Chain A Binding Site BS01

Receptor Information
>4nhm Chain A (length=546) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EDKIKGMFNPKIWDKTFQDGLKKEIEDSQPYNWGTIHELVNDDLLRAVRK
EIETEIHFTKKETDIYRVNQSGDLANLSGLDWDDLSRLPNLFKLRQILYS
KQYRDFFGYVTKAGKLSGSKTDMSINTYTKGCHLLTHDDVIGSRRISFIL
YLPDPDRKWKSHYGGGLRLFPSILPNVPHSDPSAKLVPQFNQIAFFKVLP
GFSFHDVEEVKVDKHRLSIQGWYHIPQVGEEGYIPGELEDFEFPKDERNI
LSFHEVKHFEKMLKVKLSEAEFTYLSQYISPEHLSSKGIEKLQKQFVENS
SLQIESFLNDDKSELLKKVIKQKELEQECPYHSKDVKAPWKTAIPPHKAR
YLYIDGKEYRNFQTEADILEALNNNDLPNFQFTKDAIKIISDASGNSREN
NFDAELALIDLAVFHKSTIFKKYLALLTSLCPVSEQILIRRFRPGMDFTL
ATKCRFNELLKSNPDIIDAVLEGTLCLTPSAGWESGELGGYELYMMDSVL
INDPPAWNTFNLVLRDESVLEFVKYVSWSAKSSRWDVKMKWDVKSC
Ligand information
Ligand IDUN9
InChIInChI=1S/C12H9ClN2O4/c13-11-7-4-2-1-3-6(7)10(18)9(15-11)12(19)14-5-8(16)17/h1-4,18H,5H2,(H,14,19)(H,16,17)
InChIKeyOUQVKRKGTAUJQA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)CNC(=O)c1nc(Cl)c2ccccc2c1O
OpenEye OEToolkits 1.5.0c1ccc2c(c1)c(c(nc2Cl)C(=O)NCC(=O)O)O
ACDLabs 10.04O=C(O)CNC(=O)c1nc(Cl)c2c(c1O)cccc2
FormulaC12 H9 Cl N2 O4
NameN-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE
ChEMBLCHEMBL426560
DrugBankDB08687
ZINCZINC000000007670
PDB chain4nhm Chain A Residue 701 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4nhm Structure of the Ribosomal Oxygenase OGFOD1 Provides Insights into the Regio- and Stereoselectivity of Prolyl Hydroxylases.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		N148 Y150 L156 H159 I171 Y173 L189 H227 V229 R238 Q242 W244
Binding residue
(residue number reindexed from 1)		N126 Y128 L134 H137 I149 Y151 L167 H205 V207 R216 Q220 W222
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.11.-
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0008143 poly(A) binding
GO:0008198 ferrous iron binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0031418 L-ascorbic acid binding
GO:0031543 peptidyl-proline dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0000288 nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
GO:0006415 translational termination
GO:0006449 regulation of translational termination
GO:0006450 regulation of translational fidelity
GO:0018126 protein hydroxylation
GO:0018188 peptidyl-proline di-hydroxylation
Cellular Component
GO:0005634 nucleus
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:4nhm, PDBe:4nhm, PDBj:4nhm
PDBsum4nhm
PubMed25728928
UniProtP40032|TPA1_YEAST Prolyl 3,4-dihydroxylase TPA1 (Gene Name=TPA1)

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