Structure of PDB 4ccl Chain A Binding Site BS01
Receptor Information
>4ccl Chain A (length=371) Species:
562
(Escherichia coli) [
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MEYQLTLNWPDFLERHWQKRPVVLKRGFNNFIDPISPDELAGLAMESEVD
SRLVSHQDGKWQVSHGPFESYDHLGETNWSLLVQAVNHWHEPTAALMRPF
RELPDWRIDDLMISFSVPGGGVGPHLDQYDVFIIQGTGRRRWRVGEKLQK
QHCPHPDLLQVDPFEAIIDEELEPGDILYIPPGFPHEGYALENAMNYSVG
FRAPNTRELISGFADYVLQRELGGNYYSDPDVPPRAHPADVLPQEMDKLR
EMMLELINQPEHFKQWFGEFISQSRHELDIAPPEPPYQPDEIYDALKQGE
VLVRLGGLRVLRIGDDVYANGEKIDSPHRPALDALASNIALTAENFGDAL
EDPSFLAMLAALVNSGYWFFE
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
4ccl Chain A Residue 1373 [
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Receptor-Ligand Complex Structure
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PDB
4ccl
Ribosomal oxygenases are structurally conserved from prokaryotes to humans.
Resolution
2.596 Å
Binding residue
(original residue number in PDB)
H125 D127 H187
Binding residue
(residue number reindexed from 1)
H125 D127 H186
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.14.11.47
: [50S ribosomal protein L16]-arginine 3-hydroxylase.
Gene Ontology
Molecular Function
GO:0005515
protein binding
GO:0008198
ferrous iron binding
GO:0016706
2-oxoglutarate-dependent dioxygenase activity
GO:0042803
protein homodimerization activity
GO:0046872
metal ion binding
GO:0051213
dioxygenase activity
Biological Process
GO:0043687
post-translational protein modification
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:4ccl
,
PDBe:4ccl
,
PDBj:4ccl
PDBsum
4ccl
PubMed
24814345
UniProt
P27431
|ROXA_ECOLI Ribosomal protein uL16 3-hydroxylase (Gene Name=roxA)
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