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5WY1

Crystal structure of mouse DNA methyltransferase 1 (T1505A mutant)

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 PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 2001
ChainResidue
ACYS359
ACYS362
ACYS420
AHIS424

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 2002
ChainResidue
ACYS656
ACYS659
ACYS662
ACYS694

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 2003
ChainResidue
ACYS823
ACYS897
ACYS900
AHIS796

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 2004
ChainResidue
ACYS1479
ACYS1481
ACYS1487
AHIS1504

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 Residues46
DetailsZN_FING: CXXC-type => ECO:0000255|PROSITE-ProRule:PRU00509
ChainResidueDetails
AASN649-PRO695

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:17576694
ChainResidueDetails
ACYS1229

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS359
ACYS362
ACYS420
AHIS424

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00509
ChainResidueDetails
ACYS656
ACYS659
ACYS662
ACYS667
ACYS670
ACYS673
ACYS689
ACYS694

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:4DA4
ChainResidueDetails
ASER1149

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4
ChainResidueDetails
AGLY1153
AGLU1171
AVAL1582

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9
ChainResidueDetails
AASP1193

site_idSWS_FT_FI8
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P26358
ChainResidueDetails
ALYS372
ALYS1120
ALYS1352
ALYS1418
ALYS752
ALYS895
ALYS961
ALYS965
ALYS979
ALYS1114
ALYS1116
ALYS1118

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17965600, ECO:0000269|PubMed:9211941
ChainResidueDetails
ASER515

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P26358
ChainResidueDetails
ASER555
ASER735
ASER882

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER713

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER717

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS1122
ALYS1124

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P26358
ChainResidueDetails
ALYS1611

221371

PDB entries from 2024-06-19

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