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7XIB

Cryo-EM structure of human DNMT1 (aa:351-1616) in complex with ubiquitinated H3 and hemimethylated DNA analog (CXXC-disordered form)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
A0005634cellular_componentnucleus
A0006346biological_processDNA methylation-dependent heterochromatin formation
A0008168molecular_functionmethyltransferase activity
A0008270molecular_functionzinc ion binding
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 Residues4
DetailsBINDING:
ChainResidueDetails
ACYS353
ACYS356
ACYS414
AHIS418

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00509
ChainResidueDetails
ACYS653
ACYS656
ACYS659
ACYS664
ACYS667
ACYS670
ACYS686
ACYS691

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13864
ChainResidueDetails
ASER1146
AGLY1150
AASP1190
AVAL1580

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PTA
ChainResidueDetails
AGLU1168
ACYS1191
AASN1578

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Important for activity => ECO:0000250
ChainResidueDetails
ASER509

site_idSWS_FT_FI8
Number of Residues9
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21947282
ChainResidueDetails
ALYS366
ALYS749
ALYS891
ALYS957
ALYS961
ALYS975
ALYS1054
ALYS1349
ALYS1415

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER394

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER398
ASER549
ASER878

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13864
ChainResidueDetails
ASER509

site_idSWS_FT_FI12
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_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336
ChainResidueDetails
ASER732

site_idSWS_FT_FI14
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21947282, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS1111
ALYS1113
ALYS1115

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by EHMT2 => ECO:0000269|PubMed:21947282
ChainResidueDetails
ALYS1117

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P13864
ChainResidueDetails
ALYS1119
ALYS1121

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS1609

220113

PDB entries from 2024-05-22

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