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8K62

Crystal structure of ALKBH1 and 13h complex.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000791cellular_componenteuchromatin
A0002101biological_processtRNA wobble cytosine modification
A0003824molecular_functioncatalytic activity
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006281biological_processDNA repair
A0006351biological_processDNA-templated transcription
A0006417biological_processregulation of translation
A0006446biological_processregulation of translational initiation
A0006448biological_processregulation of translational elongation
A0006974biological_processDNA damage response
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0016829molecular_functionlyase activity
A0035513biological_processoxidative RNA demethylation
A0035515molecular_functionoxidative RNA demethylase activity
A0035516molecular_functionbroad specificity oxidative DNA demethylase activity
A0042056molecular_functionchemoattractant activity
A0042245biological_processRNA repair
A0046872molecular_functionmetal ion binding
A0050918biological_processpositive chemotaxis
A0051213molecular_functiondioxygenase activity
A0070129biological_processregulation of mitochondrial translation
A0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
A0141131molecular_functionDNA N6-methyladenine demethylase activity
A0141137biological_processpositive regulation of gene expression, epigenetic
A0160290molecular_function2-oxoglutarate-dependent tRNA 5-methylcytidine formyltransferase activity
A1990983biological_processregulation of translational initiation by tRNA modification
A1990984molecular_functiontRNA demethylase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues139
DetailsDomain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q6NS38","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q96Q83","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19959401","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27745969","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Secondary catalytic residue forming the imine linkage with DNA","evidences":[{"source":"PubMed","id":"23577621","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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