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2FD8

Crystal Structure of AlkB in complex with Fe(II), 2-oxoglutarate, and methylated trinucleotide T-meA-T

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006307biological_processDNA alkylation repair
A0006974biological_processDNA damage response
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0035513biological_processoxidative RNA demethylation
A0035515molecular_functionoxidative RNA demethylase activity
A0035516molecular_functionbroad specificity oxidative DNA demethylase activity
A0035552biological_processobsolete oxidative single-stranded DNA demethylation
A0035553biological_processobsolete oxidative single-stranded RNA demethylation
A0042245biological_processRNA repair
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0070989biological_processoxidative demethylation
A0072702biological_processresponse to methyl methanesulfonate
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 300
ChainResidue
AHIS131
AASP133
AHIS187
AAKG400
AHOH671

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AKG A 400
ChainResidue
AASP133
AHIS187
AILE189
AARG204
AASN206
AARG210
AFE2300
AHOH619
AHOH671
BMA7502
ALEU118
AASN120
ATYR122
AHIS131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16482161, ECO:0000269|PubMed:20084272
ChainResidueDetails
ATRP69
AASP135
AARG161

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ATYR76
AASN120
AARG204

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:16482161
ChainResidueDetails
AHIS131
AASP133
AHIS187

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PDB entries from 2024-04-17

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