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

4H0N

Crystal structure of Spodoptera frugiperda DNMT2 E260A/E261A/K263A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003723molecular_functionRNA binding
A0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0008033biological_processtRNA processing
A0008168molecular_functionmethyltransferase activity
A0032259biological_processmethylation
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0008033biological_processtRNA processing
B0008168molecular_functionmethyltransferase activity
B0032259biological_processmethylation
C0003677molecular_functionDNA binding
C0003723molecular_functionRNA binding
C0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0008033biological_processtRNA processing
C0008168molecular_functionmethyltransferase activity
C0032259biological_processmethylation
D0003677molecular_functionDNA binding
D0003723molecular_functionRNA binding
D0003886molecular_functionDNA (cytosine-5-)-methyltransferase activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0008033biological_processtRNA processing
D0008168molecular_functionmethyltransferase activity
D0032259biological_processmethylation
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SAH A 401
ChainResidue
ATYR9
AASN55
AILE56
ASER75
APRO77
ASER97
AASN316
ASER317
AVAL318
ASER10
AGLY11
AILE12
AGLY14
AASP33
AILE34
AASN35
AARG54

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AGLY103
AASP106
BASP133
BGLU137

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SAH B 401
ChainResidue
BTYR9
BSER10
BGLY11
BILE12
BGLY13
BGLY14
BASP33
BILE34
BASN35
BASN55
BILE56
BSER75
BPRO77
BGLN79
BSER97
BASN316
BSER317

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
AASP133
AGLU137
BGLY103
BASP106
BGLN107

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE SAH C 401
ChainResidue
CTYR9
CSER10
CGLY11
CILE12
CASP33
CILE34
CARG54
CASN55
CILE56
CSER75
CPRO77
CSER97
CASN316
CSER317
CVAL318

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA C 402
ChainResidue
CGLY103
CASP106

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SAH D 401
ChainResidue
DTYR9
DSER10
DGLY11
DILE12
DGLY14
DASP33
DILE34
DASN35
DASN55
DILE56
DSER75
DPRO77
DGLN79
DSER97
DASN316
DSER317
DVAL318

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA D 402
ChainResidue
DGLY103
DASP106

Functional Information from PROSITE/UniProt
site_idPS00095
Number of Residues19
DetailsC5_MTASE_2 C-5 cytosine-specific DNA methylases C-terminal signature. RllGNSVnVkViseLlkiL
ChainResidueDetails
AARG312-LEU330

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01016
ChainResidueDetails
ACYS78
BCYS78
CCYS78
DCYS78

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:23103599, ECO:0007744|PDB:4H0N
ChainResidueDetails
AILE12
CASP33
CASN55
CASN316
DILE12
DASP33
DASN55
DASN316
AASP33
AASN55
AASN316
BILE12
BASP33
BASN55
BASN316
CILE12

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|Ref.2, ECO:0007744|PDB:4H0N
ChainResidueDetails
ASER75
DSER75
DGLN79
DSER97
AGLN79
ASER97
BSER75
BGLN79
BSER97
CSER75
CGLN79
CSER97

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon