Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5ZMD

Crystal structure of FTO in complex with m6dA modified ssDNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0001659biological_processtemperature homeostasis
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006307biological_processDNA alkylation repair
A0008198molecular_functionferrous iron binding
A0010883biological_processregulation of lipid storage
A0016180biological_processsnRNA processing
A0016491molecular_functionoxidoreductase activity
A0016607cellular_componentnuclear speck
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0016740molecular_functiontransferase activity
A0035515molecular_functionoxidative RNA demethylase activity
A0035516molecular_functionbroad specificity oxidative DNA demethylase activity
A0040014biological_processregulation of multicellular organism growth
A0042245biological_processRNA repair
A0044065biological_processregulation of respiratory system process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0060612biological_processadipose tissue development
A0061157biological_processmRNA destabilization
A0070350biological_processregulation of white fat cell proliferation
A0090335biological_processregulation of brown fat cell differentiation
A1990931molecular_functionmRNA N6-methyladenosine dioxygenase activity
A1990984molecular_functiontRNA demethylase activity
C0001659biological_processtemperature homeostasis
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006307biological_processDNA alkylation repair
C0008198molecular_functionferrous iron binding
C0010883biological_processregulation of lipid storage
C0016180biological_processsnRNA processing
C0016491molecular_functionoxidoreductase activity
C0016607cellular_componentnuclear speck
C0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
C0016740molecular_functiontransferase activity
C0035515molecular_functionoxidative RNA demethylase activity
C0035516molecular_functionbroad specificity oxidative DNA demethylase activity
C0040014biological_processregulation of multicellular organism growth
C0042245biological_processRNA repair
C0044065biological_processregulation of respiratory system process
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
C0060612biological_processadipose tissue development
C0061157biological_processmRNA destabilization
C0070350biological_processregulation of white fat cell proliferation
C0090335biological_processregulation of brown fat cell differentiation
C1990931molecular_functionmRNA N6-methyladenosine dioxygenase activity
C1990984molecular_functiontRNA demethylase activity
E0001659biological_processtemperature homeostasis
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006307biological_processDNA alkylation repair
E0008198molecular_functionferrous iron binding
E0010883biological_processregulation of lipid storage
E0016180biological_processsnRNA processing
E0016491molecular_functionoxidoreductase activity
E0016607cellular_componentnuclear speck
E0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
E0016740molecular_functiontransferase activity
E0035515molecular_functionoxidative RNA demethylase activity
E0035516molecular_functionbroad specificity oxidative DNA demethylase activity
E0040014biological_processregulation of multicellular organism growth
E0042245biological_processRNA repair
E0044065biological_processregulation of respiratory system process
E0046872molecular_functionmetal ion binding
E0051213molecular_functiondioxygenase activity
E0060612biological_processadipose tissue development
E0061157biological_processmRNA destabilization
E0070350biological_processregulation of white fat cell proliferation
E0090335biological_processregulation of brown fat cell differentiation
E1990931molecular_functionmRNA N6-methyladenosine dioxygenase activity
E1990984molecular_functiontRNA demethylase activity
G0001659biological_processtemperature homeostasis
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006307biological_processDNA alkylation repair
G0008198molecular_functionferrous iron binding
G0010883biological_processregulation of lipid storage
G0016180biological_processsnRNA processing
G0016491molecular_functionoxidoreductase activity
G0016607cellular_componentnuclear speck
G0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
G0016740molecular_functiontransferase activity
G0035515molecular_functionoxidative RNA demethylase activity
G0035516molecular_functionbroad specificity oxidative DNA demethylase activity
G0040014biological_processregulation of multicellular organism growth
G0042245biological_processRNA repair
G0044065biological_processregulation of respiratory system process
G0046872molecular_functionmetal ion binding
G0051213molecular_functiondioxygenase activity
G0060612biological_processadipose tissue development
G0061157biological_processmRNA destabilization
G0070350biological_processregulation of white fat cell proliferation
G0090335biological_processregulation of brown fat cell differentiation
G1990931molecular_functionmRNA N6-methyladenosine dioxygenase activity
G1990984molecular_functiontRNA demethylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MN A 1001
ChainResidue
AHIS231
AASP233
AHIS307
AOGA1002

site_idAC2
Number of Residues12
Detailsbinding site for residue OGA A 1002
ChainResidue
AHIS307
AVAL309
AARG316
ASER318
ATHR320
AARG322
AMN1001
AARG96
AASN205
AHIS231
AASP233
ATYR295

site_idAC3
Number of Residues4
Detailsbinding site for residue MN C 1001
ChainResidue
CHIS231
CASP233
CHIS307
COGA1002

site_idAC4
Number of Residues12
Detailsbinding site for residue OGA C 1002
ChainResidue
CARG96
CASN205
CHIS231
CASP233
CVAL272
CTYR295
CHIS307
CVAL309
CARG316
CSER318
CARG322
CMN1001

site_idAC5
Number of Residues4
Detailsbinding site for residue MN E 1001
ChainResidue
EHIS231
EASP233
EHIS307
EOGA1002

site_idAC6
Number of Residues12
Detailsbinding site for residue OGA E 1002
ChainResidue
EARG96
EASN205
EHIS231
ETYR295
EHIS307
EVAL309
EARG316
ESER318
ETHR320
EARG322
EMN1001
F6MA5

site_idAC7
Number of Residues4
Detailsbinding site for residue MN G 1001
ChainResidue
GHIS231
GASP233
GHIS307
GOGA1002

site_idAC8
Number of Residues11
Detailsbinding site for residue OGA G 1002
ChainResidue
GARG96
GASN205
GHIS231
GVAL272
GTYR295
GHIS307
GVAL309
GARG316
GSER318
GARG322
GMN1001

site_idAC9
Number of Residues18
Detailsbinding site for Di-peptide GLU C 375 and ARG C 449
ChainResidue
CHIS371
CASN372
CGLU373
CVAL374
CPHE376
CGLU377
CLEU379
CARG380
CTRP407
CARG445
CGLN446
CASN447
CLEU448
CARG450
CGLU451
CTRP452
CHIS453
CPHE487

site_idAD1
Number of Residues16
Detailsbinding site for Di-nucleotide DT D 4 and 6MA D 5
ChainResidue
BDT4
CILE85
CLYS86
CARG96
CTYR108
CLEU109
CASN110
CVAL228
CSER229
CTRP230
CHIS231
CGLU234
CLYS306
CARG322
DDC3
DDT6

site_idAD2
Number of Residues16
Detailsbinding site for Di-nucleotide 6MA D 5 and DT D 6
ChainResidue
CLYS88
CARG96
CTYR108
CLEU109
CLYS216
CVAL228
CSER229
CTRP230
CHIS231
CGLU234
CLYS306
CARG322
DDT4
DDA7
BDT6
CILE85

site_idAD3
Number of Residues9
Detailsbinding site for Di-peptide LYS E 107 and GLU E 377
ChainResidue
ETYR106
ETYR108
EARG112
EASN235
EGLU373
EGLU375
EPHE376
ETRP378
EGLN381

site_idAD4
Number of Residues8
Detailsbinding site for Di-peptide LEU E 464 and LYS E 469
ChainResidue
EILE460
EARG462
ETHR463
EPRO465
EALA466
EGLN468
EPRO470
EGLU471

site_idAD5
Number of Residues15
Detailsbinding site for Di-nucleotide DT F 4 and 6MA F 5
ChainResidue
ELYS86
EARG96
ETYR106
ETYR108
ELEU109
EASN110
EVAL228
ESER229
ETRP230
EHIS231
EGLU234
EOGA1002
FDC3
FDT6
HDT4

site_idAD6
Number of Residues17
Detailsbinding site for Di-nucleotide 6MA F 5 and DT F 6
ChainResidue
EILE85
ELYS86
ELYS88
EARG96
ETYR106
ETYR108
ELEU109
ELYS216
EVAL228
ESER229
ETRP230
EHIS231
EGLU234
EOGA1002
FDT4
FDA7
HDT6

site_idAD7
Number of Residues14
Detailsbinding site for Di-nucleotide DT H 4 and 6MA H 5
ChainResidue
FDT4
GILE85
GLYS86
GARG96
GTYR108
GLEU109
GASN110
GVAL228
GSER229
GTRP230
GHIS231
GGLU234
HDC3
HDT6

site_idAD8
Number of Residues14
Detailsbinding site for Di-nucleotide 6MA H 5 and DT H 6
ChainResidue
FDT6
GILE85
GLYS86
GARG96
GTYR108
GLEU109
GLYS216
GVAL228
GSER229
GTRP230
GHIS231
GGLU234
HDT4
HDA7

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0007744|PDB:3LFM
ChainResidueDetails
AARG96
GARG96
GTYR108
GTHR320
ATYR108
ATHR320
CARG96
CTYR108
CTHR320
EARG96
ETYR108
ETHR320

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:25452335, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4QKN
ChainResidueDetails
AASN205
CASN205
EASN205
GASN205

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:25452335, ECO:0000305|PubMed:23547775, ECO:0000305|PubMed:25452335, ECO:0000305|PubMed:26457839, ECO:0000305|PubMed:28553460, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4CXW, ECO:0007744|PDB:4CXX, ECO:0007744|PDB:4CXY, ECO:0007744|PDB:4IDZ, ECO:0007744|PDB:4IE0, ECO:0007744|PDB:4IE4, ECO:0007744|PDB:4IE5, ECO:0007744|PDB:4IE6, ECO:0007744|PDB:4IE7, ECO:0007744|PDB:4QKN, ECO:0007744|PDB:4ZS2, ECO:0007744|PDB:4ZS3
ChainResidueDetails
AHIS231
CHIS231
EHIS231
GHIS231

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000305|PubMed:23547775, ECO:0000305|PubMed:25452335, ECO:0000305|PubMed:26457839, ECO:0000305|PubMed:28553460, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4CXW, ECO:0007744|PDB:4CXX, ECO:0007744|PDB:4CXY, ECO:0007744|PDB:4IDZ, ECO:0007744|PDB:4IE0, ECO:0007744|PDB:4IE4, ECO:0007744|PDB:4IE5, ECO:0007744|PDB:4IE6, ECO:0007744|PDB:4IE7, ECO:0007744|PDB:4QKN, ECO:0007744|PDB:4ZS2, ECO:0007744|PDB:4ZS3
ChainResidueDetails
AASP233
AHIS307
CASP233
CHIS307
EASP233
EHIS307
GASP233
GHIS307

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:25452335, ECO:0000269|PubMed:26457839, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4QKN, ECO:0007744|PDB:4ZS2, ECO:0007744|PDB:4ZS3
ChainResidueDetails
ATYR295
AARG316
CTYR295
CARG316
ETYR295
EARG316
GTYR295
GARG316

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20376003, ECO:0000269|PubMed:25452335, ECO:0000269|PubMed:26457839, ECO:0007744|PDB:3LFM, ECO:0007744|PDB:4QKN, ECO:0007744|PDB:4ZS2
ChainResidueDetails
AARG322
CARG322
EARG322
GARG322

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS216
CLYS216
ELYS216
GLYS216

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon