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1D2C

METHYLTRANSFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005542molecular_functionfolic acid binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005977biological_processglycogen metabolic process
A0006111biological_processregulation of gluconeogenesis
A0006544biological_processglycine metabolic process
A0006555biological_processmethionine metabolic process
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0016594molecular_functionglycine binding
A0016740molecular_functiontransferase activity
A0017174molecular_functionglycine N-methyltransferase activity
A0032259biological_processmethylation
A0034708cellular_componentmethyltransferase complex
A0042802molecular_functionidentical protein binding
A0046498biological_processS-adenosylhomocysteine metabolic process
A0046500biological_processS-adenosylmethionine metabolic process
A0051289biological_processprotein homotetramerization
A0098603molecular_functionselenol Se-methyltransferase activity
A0170033biological_processL-amino acid metabolic process
A0170039biological_processproteinogenic amino acid metabolic process
A1901052biological_processsarcosine metabolic process
A1904047molecular_functionS-adenosyl-L-methionine binding
B0005542molecular_functionfolic acid binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005977biological_processglycogen metabolic process
B0006111biological_processregulation of gluconeogenesis
B0006544biological_processglycine metabolic process
B0006555biological_processmethionine metabolic process
B0006730biological_processone-carbon metabolic process
B0008168molecular_functionmethyltransferase activity
B0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
B0016594molecular_functionglycine binding
B0016740molecular_functiontransferase activity
B0017174molecular_functionglycine N-methyltransferase activity
B0032259biological_processmethylation
B0034708cellular_componentmethyltransferase complex
B0042802molecular_functionidentical protein binding
B0046498biological_processS-adenosylhomocysteine metabolic process
B0046500biological_processS-adenosylmethionine metabolic process
B0051289biological_processprotein homotetramerization
B0098603molecular_functionselenol Se-methyltransferase activity
B0170033biological_processL-amino acid metabolic process
B0170039biological_processproteinogenic amino acid metabolic process
B1901052biological_processsarcosine metabolic process
B1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22037183, ECO:0000312|PDB:3THR, ECO:0000312|PDB:3THS
ChainResidueDetails
ASER3
AHIS214
AARG239
BSER3
BHIS214
BARG239

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22037183, ECO:0000312|PDB:3THS
ChainResidueDetails
ATYR5
BTYR5

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12859184, ECO:0007744|PDB:1NBH
ChainResidueDetails
ATYR21
BTYR21

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12859184, ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI
ChainResidueDetails
ATRP30
AARG40
AASP85
AASN116
BTRP30
BARG40
BASP85
BASN116

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8810903, ECO:0007744|PDB:1XVA
ChainResidueDetails
ATYR33
AARG175
ATYR220
BTYR33
BARG175
BTYR220

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12859184, ECO:0000269|PubMed:8810903, ECO:0000312|PDB:1XVA, ECO:0007744|PDB:1NBH, ECO:0007744|PDB:1NBI
ChainResidueDetails
AALA64
BALA64

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12859184, ECO:0000269|PubMed:8810903, ECO:0007744|PDB:1NBI, ECO:0007744|PDB:1XVA
ChainResidueDetails
ALEU136
BLEU136

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N-acetylvaline => ECO:0000269|PubMed:2822402
ChainResidueDetails
AVAL1
BVAL1

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QXF8
ChainResidueDetails
ASER9
BSER9

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXF8
ChainResidueDetails
ATYR33
BTYR33

site_idSWS_FT_FI11
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXF8
ChainResidueDetails
ALYS45
ALYS190
ALYS195
ALYS200
BLYS45
BLYS190
BLYS195
BLYS200

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xva
ChainResidueDetails
AGLU15

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xva
ChainResidueDetails
BGLU15

site_idMCSA1
Number of Residues5
DetailsM-CSA 23
ChainResidueDetails
ATYR21electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AGLY137electrostatic stabiliser, hydrogen bond acceptor
AHIS142activator
AARG175electrostatic stabiliser
ATYR194electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 23
ChainResidueDetails
BTYR21electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BGLY137electrostatic stabiliser, hydrogen bond acceptor
BHIS142activator
BARG175electrostatic stabiliser
BTYR194electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

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PDB entries from 2025-06-11

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