Structure of PDB 3thp Chain A Binding Site BS02

Receptor Information
>3thp Chain A (length=304) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TLLRHEGIETVSYATQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMP
PNKPYSFARYRTTEESKRAYVTLNGKEVVDDLGQKITLYLNFVEKVQWKE
LRPQALPPGLMVVEEIISSEEEKMLLESVRRVKHFGYKDKPLSGGLPDIC
ESFLEKWLRKGYIKHKPDQMTINQYEPGQGIPAHIDTHSAFEDEIVSLSL
GSEIVMDFKHPDGIAVPVMLPRRSLLVMTGESRYLWTHGITCRKFDTVQA
SEKSGIITSDVGDLTLSKRGLRTSFTFRKVRQTPCNCSYPLVCDSQRKEN
LYFQ
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain3thp Chain A Residue 402 [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]
PDB3thp Crystal structure and RNA binding properties of the RNA recognition motif (RRM) and AlkB domains in human AlkB homolog 8 (ABH8), an enzyme catalyzing tRNA hypermodification.
Resolution3.2 Å
Binding residue
(original residue number in PDB)
H238 D240 H292
Binding residue
(residue number reindexed from 1)
H184 D186 H238
Annotation score1
Enzymatic activity
Enzyme Commision number 2.1.1.229: tRNA (carboxymethyluridine(34)-5-O)-methyltransferase.
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0003723 RNA binding
Biological Process
GO:0070988 demethylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3thp, PDBe:3thp, PDBj:3thp
PDBsum3thp
PubMed22065580
UniProtQ96BT7|ALKB8_HUMAN Alkylated DNA repair protein alkB homolog 8 (Gene Name=ALKBH8)

[Back to BioLiP]