Structure of PDB 4nhl Chain A Binding Site BS02

Receptor Information
>4nhl 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 IDOGA
InChIInChI=1S/C4H5NO5/c6-2(7)1-5-3(8)4(9)10/h1H2,(H,5,8)(H,6,7)(H,9,10)
InChIKeyBIMZLRFONYSTPT-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)CNC(=O)C(O)=O
ACDLabs 10.04O=C(O)C(=O)NCC(=O)O
OpenEye OEToolkits 1.5.0C(C(=O)O)NC(=O)C(=O)O
FormulaC4 H5 N O5
NameN-OXALYLGLYCINE
ChEMBLCHEMBL90852
DrugBank
ZINCZINC000001534133
PDB chain4nhl Chain A Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4nhl Structure of the Ribosomal Oxygenase OGFOD1 Provides Insights into the Regio- and Stereoselectivity of Prolyl Hydroxylases.
Resolution2.84 Å
Binding residue
(original residue number in PDB)		L156 H159 Y173 H227 V229 R238 Q242
Binding residue
(residue number reindexed from 1)		L134 H137 Y151 H205 V207 R216 Q220
Annotation score2
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:4nhl, PDBe:4nhl, PDBj:4nhl
PDBsum4nhl
PubMed25728928
UniProtP40032|TPA1_YEAST Prolyl 3,4-dihydroxylase TPA1 (Gene Name=TPA1)

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