Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4DA4

Structure of mouse DNMT1 (731-1602) bound to hemimethylated CpG DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003682molecular_functionchromatin binding
A0008168molecular_functionmethyltransferase activity
B0003682molecular_functionchromatin binding
B0008168molecular_functionmethyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 1701
ChainResidue
APHE1148
AASP1193
ACYS1194
AGLY1226
ALYS1247
ALEU1250
AALA1581
AVAL1582
AHOH1805
AHOH1808
AHOH1834
ASER1149
AHOH1900
DC4918
AGLY1150
AGLY1152
AGLY1153
ALEU1154
AGLU1171
AMET1172
ATRP1173

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1702
ChainResidue
ACYS1479
ACYS1481
ACYS1487
AHIS1504

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1703
ChainResidue
AHIS796
ACYS823
ACYS897
ACYS900

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE SAH B 1701
ChainResidue
BPHE1148
BSER1149
BGLY1150
BGLY1152
BGLY1153
BLEU1154
BGLU1171
BMET1172
BTRP1173
BASP1193
BCYS1194
BGLY1226
BLYS1247
BLEU1250
BALA1581
BVAL1582
BHOH1875
BHOH1903
BHOH1940
BHOH1963
BHOH2009
BHOH2153
FC4918

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1702
ChainResidue
BCYS1479
BCYS1481
BCYS1487
BHIS1504

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1703
ChainResidue
BHIS796
BCYS823
BCYS897
BCYS900

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT B 1704
ChainResidue
AARG1566
APHE1568
AGLY1569
AARG1574
AHOH1910
AHOH2182
BARG1566
BPHE1567
BPHE1568
BGLY1569
BARG1574
BHOH1840
BHOH2039

Functional Information from PROSITE/UniProt
site_idPS00094
Number of Residues13
DetailsC5_MTASE_1 C-5 cytosine-specific DNA methylases active site. EmLcgGpPCqGFS
ChainResidueDetails
AGLU1221-SER1233

site_idPS00095
Number of Residues19
DetailsC5_MTASE_2 C-5 cytosine-specific DNA methylases C-terminal signature. RqvGNAVpPpLakaIgleI
ChainResidueDetails
AARG1576-ILE1594

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:17576694
ChainResidueDetails
ACYS1229
BCYS1229

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:4DA4
ChainResidueDetails
ASER1149
BSER1149

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4
ChainResidueDetails
AGLY1153
AGLU1171
AVAL1582
BGLY1153
BGLU1171
BVAL1582

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9
ChainResidueDetails
AASP1193
BASP1193

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P26358
ChainResidueDetails
ASER735
ASER882
BSER735
BSER882

site_idSWS_FT_FI6
Number of Residues22
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P26358
ChainResidueDetails
ALYS752
ALYS1352
ALYS1418
BLYS752
BLYS895
BLYS961
BLYS965
BLYS979
BLYS1114
BLYS1116
BLYS1118
ALYS895
BLYS1120
BLYS1352
BLYS1418
ALYS961
ALYS965
ALYS979
ALYS1114
ALYS1116
ALYS1118
ALYS1120

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS1122
ALYS1124
BLYS1122
BLYS1124

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon