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3PTA

Crystal structure of human DNMT1(646-1600) in complex with DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0008168molecular_functionmethyltransferase activity
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SAH A 1601
ChainResidue
APHE1145
ACYS1191
APRO1225
ALEU1247
AGLU1266
AASN1578
AALA1579
AVAL1580
ASER1146
AGLY1147
AGLY1150
ALEU1151
AGLU1168
AMET1169
ATRP1170
AGLU1189

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
ACYS1476
ACYS1478
ACYS1485
AHIS1502

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
ACYS653
ACYS656
ACYS659
ACYS691

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 3
ChainResidue
AHIS793
ACYS820
ACYS893
ACYS896

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 5
ChainResidue
ACYS664
ACYS667
ACYS670
ACYS686
AGLN687

Functional Information from PROSITE/UniProt
site_idPS00094
Number of Residues13
DetailsC5_MTASE_1 C-5 cytosine-specific DNA methylases active site. EmLcgGpPCqGFS
ChainResidueDetails
AGLU1218-SER1230

site_idPS00095
Number of Residues19
DetailsC5_MTASE_2 C-5 cytosine-specific DNA methylases C-terminal signature. RqvGNAVpPpLakaIgleI
ChainResidueDetails
AARG1574-ILE1592

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsZN_FING: CXXC-type => ECO:0000255|PROSITE-ProRule:PRU00509
ChainResidueDetails
AASN646-PRO692

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE:
ChainResidueDetails
ACYS1226

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00509
ChainResidueDetails
ACYS653
ACYS656
ACYS659
ACYS664
ACYS667
ACYS670
ACYS686
ACYS691

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13864
ChainResidueDetails
ASER1146
AGLY1150
AASP1190
AVAL1580

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PTA
ChainResidueDetails
AGLU1168
ACYS1191
AASN1578

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER714

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336
ChainResidueDetails
ASER732

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21947282
ChainResidueDetails
ALYS749
ALYS891
ALYS957
ALYS961
ALYS975
ALYS1054
ALYS1349
ALYS1415

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER878

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21947282, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1111
ALYS1113
ALYS1115

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by EHMT2 => ECO:0000269|PubMed:21947282
ChainResidueDetails
ALYS1117

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P13864
ChainResidueDetails
ALYS1119
ALYS1121

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PDB entries from 2024-07-10

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