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4WXX

The crystal structure of human DNMT1(351-1600)

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
B0003677molecular_functionDNA binding
B0003682molecular_functionchromatin binding
B0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
B0005634cellular_componentnucleus
B0006346biological_processDNA methylation-dependent heterochromatin formation
B0008168molecular_functionmethyltransferase activity
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1701
ChainResidue
ACYS1476
ACYS1478
ACYS1485
AHIS1502

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1702
ChainResidue
AHIS793
ACYS820
ACYS893
ACYS896

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN A 1703
ChainResidue
AGLY665
ACYS667
ACYS670
ACYS686
ACYS664

site_idAC4
Number of Residues5
Detailsbinding site for residue ZN A 1704
ChainResidue
ACYS653
AGLY654
ACYS656
ACYS659
ACYS691

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 1705
ChainResidue
ACYS353
ACYS356
ACYS414
AHIS418

site_idAC6
Number of Residues19
Detailsbinding site for residue SAH A 1706
ChainResidue
APHE1145
ASER1146
AGLY1147
ACYS1148
AGLY1150
ALEU1151
AGLU1168
AMET1169
ATRP1170
AGLU1189
AASP1190
ACYS1191
AGLY1223
ALEU1247
AASN1578
AALA1579
AVAL1580
AHOH1918
AHOH2051

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 1701
ChainResidue
BCYS1476
BCYS1478
BCYS1485
BHIS1502

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 1702
ChainResidue
BHIS793
BCYS820
BCYS893
BCYS896

site_idAC9
Number of Residues6
Detailsbinding site for residue ZN B 1703
ChainResidue
BCYS664
BGLY665
BCYS667
BCYS670
BCYS686
BGLN687

site_idAD1
Number of Residues5
Detailsbinding site for residue ZN B 1704
ChainResidue
BCYS653
BGLY654
BCYS656
BCYS659
BCYS691

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN B 1705
ChainResidue
BCYS353
BCYS356
BCYS414
BHIS418

site_idAD3
Number of Residues17
Detailsbinding site for residue SAH B 1706
ChainResidue
BPHE1145
BSER1146
BGLY1147
BGLY1150
BLEU1151
BGLU1168
BMET1169
BTRP1170
BGLU1189
BASP1190
BCYS1191
BGLY1223
BLEU1247
BASN1578
BALA1579
BVAL1580
BHOH1974

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 Residues92
DetailsZN_FING: CXXC-type => ECO:0000255|PROSITE-ProRule:PRU00509
ChainResidueDetails
AGLY982-HIS1028
BGLY982-HIS1028

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
ATHR1562
BTHR1562

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AARG689
APRO692
AVAL750
AALA754
BARG689
BPRO692
BVAL750
BALA754

site_idSWS_FT_FI4
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00509
ChainResidueDetails
AGLU989
BARG992
BARG995
BPHE1000
BLYS1003
BASN1006
BTYR1022
BTHR1027
AARG992
AARG995
APHE1000
ALYS1003
AASN1006
ATYR1022
ATHR1027
BGLU989

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13864
ChainResidueDetails
AGLY1482
AASP1486
ATHR1526
BGLY1482
BASP1486
BTHR1526

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PTA
ChainResidueDetails
AGLY1504
AVAL1527
BGLY1504
BVAL1527

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Important for activity => ECO:0000250
ChainResidueDetails
AMET845
BMET845

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6,N6-dimethyllysine => ECO:0000269|PubMed:18438403
ChainResidueDetails
ALYS406
BLYS406

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
AGLU463
BGLU463

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
APHE469
BPHE469

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
AGLU473
AMET502
BGLU473
BMET502

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13864
ChainResidueDetails
AILE477
AMET845
BILE477
BMET845

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-methyllysine; by SETD7 => ECO:0000269|PubMed:21151116
ChainResidueDetails
AGLY478
BGLY478

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKB/AKT1 => ECO:0000269|PubMed:21151116, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
APHE479
BPHE479

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ALEU488
BLEU488

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21565170, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
AASP490
BASP490

site_idSWS_FT_FI17
Number of Residues18
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21947282
ChainResidueDetails
AALA496
BALA496
BTYR524
BASP702
BPHE1085
BGLN1227
BGLN1293
BGLY1297
BARG1311
BGLY1390
ATYR524
AASP702
APHE1085
AGLN1227
AGLN1293
AGLY1297
AARG1311
AGLY1390

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ASER509
BSER509

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:21947282
ChainResidueDetails
AARG595
BARG595

site_idSWS_FT_FI20
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
APHE648
AVAL734
ATHR885
ALYS1214
BPHE648
BVAL734
BTHR885
BLYS1214

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
AARG730
BARG730

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
AVAL1050
BVAL1050

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336
ChainResidueDetails
ALEU1068
BLEU1068

site_idSWS_FT_FI24
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21947282, ECO:0007744|PubMed:19608861
ChainResidueDetails
ASER1447
AGLY1449
AMET1451
BSER1447
BGLY1449
BMET1451

site_idSWS_FT_FI25
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; by EHMT2 => ECO:0000269|PubMed:21947282
ChainResidueDetails
AARG1453
BARG1453

site_idSWS_FT_FI26
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P13864
ChainResidueDetails
ALEU1455
ATYR1457
BLEU1455
BTYR1457

site_idSWS_FT_FI27
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
AARG595
BARG595

224572

PDB entries from 2024-09-04

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