Structure of PDB 4bxf Chain B Binding Site BS01
Receptor Information
>4bxf Chain B (length=422) Species:
9606
(Homo sapiens) [
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SALNFDSPSSLFESLISPIKTETFFKEFWEQKPLLIQRDDPALATYYGSL
FKLTDLKSLCSRGMYYGRDVNVCRCVNGKKKVLNKDGKAHFLQLRKDFDQ
KRATIQFHQPQRFKDELWRIQEKLECYFGSLVGSNVYITPAGSQGLPPHY
DDVEVFILQLEGEKHWRLYHPTVPLARECSVEAEERIGRPVHEFMLKPGD
LLYFPRGTIHQADTPAGLAHSTHVTISTYQNNSWGDFLLDTISGLVFDTA
KEDVELRTGIPRQLLLQVESTTVATRRLSGFLRTLADRLEGTKELLSSDM
KKDFIMHRLPPYSAGDGAELSTPGGKLPRLDSVVRLQFKDHIVLTVLPQE
KMVYIYHSLKNSRETHMMTEFHGLRFPLSHLDALKQIWNSPAISVKDLKL
TTDEEKESLVLSLWTECLIQVV
Ligand information
>4bxf Chain D (length=8) Species:
9606
(Homo sapiens) [
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GCLHHHRI
Receptor-Ligand Complex Structure
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PDB
4bxf
Ribosomal oxygenases are structurally conserved from prokaryotes to humans.
Resolution
2.05 Å
Binding residue
(original residue number in PDB)
Q136 H138 Q139 L161 N165 Y167 H179 D181 C209 T255 S257 Q260 D333 H337 M405 M406
Binding residue
(residue number reindexed from 1)
Q106 H108 Q109 L131 N135 Y137 H149 D151 C179 T225 S227 Q230 D303 H307 M367 M368
Enzymatic activity
Enzyme Commision number
1.14.11.79
: protein-L-histidine (3S)-3-hydroxylase.
Gene Ontology
Molecular Function
GO:0003714
transcription corepressor activity
GO:0005515
protein binding
GO:0032452
histone demethylase activity
GO:0032453
histone H3K4 demethylase activity
GO:0036139
peptidyl-histidine dioxygenase activity
GO:0042802
identical protein binding
GO:0046872
metal ion binding
GO:0051213
dioxygenase activity
GO:0051864
histone H3K36 demethylase activity
Biological Process
GO:0006338
chromatin remodeling
GO:0042254
ribosome biogenesis
GO:0045892
negative regulation of DNA-templated transcription
Cellular Component
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005667
transcription regulator complex
GO:0005730
nucleolus
GO:0005829
cytosol
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:4bxf
,
PDBe:4bxf
,
PDBj:4bxf
PDBsum
4bxf
PubMed
24814345
UniProt
Q8IUF8
|RIOX2_HUMAN Ribosomal oxygenase 2 (Gene Name=RIOX2)
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