Structure of PDB 3kt1 Chain A Binding Site BS01

Receptor Information
>3kt1 Chain A (length=557) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DKIKGMFNPKIWDKTFQDGLKKEIEDSQPYNWGTIHELVNDDLLRAVRKE
IETEIHFTKKETDIYRVNQSGDLANLSGLDWDDLSRLPNLFKLRQILYSK
QYRDFFGYVTKAGKLSGSKTDMSINTYTKGCHLLTHDDVIGSRRISFILY
LPDPDRKWKSHYGGGLRLFPSILPNVPHSDPSAKLVPQFNQIAFFKVLPG
FSFHDVEEVKVDKHRLSIQGWYHIPQVGEEGYIPGEEEAWVRNNTNVLED
FEFPKDERNILSFHEVKHFEKMLKVKLSEAEFTYLSQYISPEHLSSKGIE
KLQKQFVENSSLQIESFLNDDKSELLKKVIKQKELEQECPYHSKDVKAPW
KTAIPPHKARYLYIDGKEYRNFQTEADILEALNNNDLPNFQFTKDAIKII
SDASGNSRENNFDAELALIDLAVFHKSTIFKKYLALLTSLCPVSEQILIR
RFRPGMDFTLATKCRFNELLKSNPDIIDAVLEGTLCLTPSAGWESGELGG
YELYMMDDSVLINDPPAWNTFNLVLRDESVLEFVKYVSWSAKSSRWDVKM
KWDVKSC
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain3kt1 Chain A Residue 653 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3kt1 Crystal structure of Tpa1 from Saccharomyces cerevisiae, a component of the messenger ribonucleoprotein complex
Resolution2.5 Å
Binding residue
(original residue number in PDB)
H159 D161 H227
Binding residue
(residue number reindexed from 1)
H136 D138 H204
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3kt1, PDBe:3kt1, PDBj:3kt1
PDBsum3kt1
PubMed20040577
UniProtP40032|TPA1_YEAST Prolyl 3,4-dihydroxylase TPA1 (Gene Name=TPA1)

[Back to BioLiP]