Structure of PDB 3kt4 Chain A

Receptor sequence
>3kt4A (length=563) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
EEDKIKGMFNPKIWDKTFQDGLKKEIEDSQPYNWGTIHELVNDDLLRAVR
KEIETEIHFTKKETDIYRVNQSGSGLDWDDLSRLPNLFKLRQILYSKQYR
DFFGYVTKAGKLSGSKTDMSINTYTKGCHLLTHDDVIGSRRISFILYLPD
PDRKWKSHYGGGLRLFPSILPNVPHSDPSAKLVPQFNQIAFFKVLPGFSF
HDVEEVKVDKHRLSIQGWYHIPQVGEEGYIPGEEEAWVRNNTSTLAQIES
NVLEDFEFPKDERNILSFHEVKHFEKMLKVKLSEAEFTYLSQYISPEHLS
SKGIEKLQKQFVENSSLQIESFLNDDKSELLKKVIKQKELEQECPYHSKD
VKAPWKTAIPPHKARYLYIDGKEYRNFQTEADILEALNNNDLPNFQFTKD
AIKIISDASGNSRENNFDAELALIDLAVFHKSTIFKKYLALLTSLCPVSE
QILIRRFRPGMDFTLATKCRFNELLKSNPDIIDAVLEGTLCLTPSAGWES
GELGGYELYMMDDSVLINDPPAWNTFNLVLRDESVLEFVKYVSWSAKSSR
WDVKMKWDVKSCD
3D structure
PDB3kt4 Crystal structure of Tpa1 from Saccharomyces cerevisiae, a component of the messenger ribonucleoprotein complex
ChainA
Resolution2.73 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 FE A H159 D161 H227 H133 D135 H201
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:3kt4, PDBe:3kt4, PDBj:3kt4
PDBsum3kt4
PubMed20040577
UniProtP40032|TPA1_YEAST Prolyl 3,4-dihydroxylase TPA1 (Gene Name=TPA1)

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