Structure of PDB 4nhk Chain A

Receptor sequence
>4nhkA (length=546) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
EDKIKGMFNPKIWDKTFQDGLKKEIEDSQPYNWGTIHELVNDDLLRAVRK
EIETEIHFTKKETDIYRVNQSGDLANLSGLDWDDLSRLPNLFKLRQILYS
KQYRDFFGYVTKAGKLSGSKTDMSINTYTKGCHLLTHDDVIGSRRISFIL
YLPDPDRKWKSHYGGGLRLFPSILPNVPHSDPSAKLVPQFNQIAFFKVLP
GFSFHDVEEVKVDKHRLSIQGWYHIPQVGEEGYIPGELEDFEFPKDERNI
LSFHEVKHFEKMLKVKLSEAEFTYLSQYISPEHLSSKGIEKLQKQFVENS
SLQIESFLNDDKSELLKKVIKQKELEQECPYHSKDVKAPWKTAIPPHKAR
YLYIDGKEYRNFQTEADILEALNNNDLPNFQFTKDAIKIISDASGNSREN
NFDAELALIDLAVFHKSTIFKKYLALLTSLCPVSEQILIRRFRPGMDFTL
ATKCRFNELLKSNPDIIDAVLEGTLCLTPSAGWESGELGGYELYMMDSVL
INDPPAWNTFNLVLRDESVLEFVKYVSWSAKSSRWDVKMKWDVKSC
3D structure
PDB4nhk Structure of the Ribosomal Oxygenase OGFOD1 Provides Insights into the Regio- and Stereoselectivity of Prolyl Hydroxylases.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN A H159 D161 H227 H137 D139 H205
BS02 PD2 A L156 H159 I171 H227 V229 S240 Q242 L134 H137 I149 H205 V207 S218 Q220
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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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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