Structure of PDB 4nhk Chain A Binding Site BS01

Receptor Information
>4nhk 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 IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain4nhk Chain A Residue 701 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4nhk 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)		H159 D161 H227
Binding residue
(residue number reindexed from 1)		H137 D139 H205
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:4nhk, PDBe:4nhk, PDBj:4nhk
PDBsum4nhk
PubMed25728928
UniProtP40032|TPA1_YEAST Prolyl 3,4-dihydroxylase TPA1 (Gene Name=TPA1)

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