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1R74

Crystal Structure of Human Glycine N-Methyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005542molecular_functionfolic acid binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005977biological_processglycogen metabolic process
A0006111biological_processregulation of gluconeogenesis
A0006555biological_processmethionine metabolic process
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0016594molecular_functionglycine binding
A0017174molecular_functionglycine N-methyltransferase activity
A0032259biological_processmethylation
A0036211biological_processprotein modification process
A0042802molecular_functionidentical protein binding
A0046498biological_processS-adenosylhomocysteine metabolic process
A0046500biological_processS-adenosylmethionine metabolic process
A0051289biological_processprotein homotetramerization
A1901052biological_processsarcosine metabolic process
A1904047molecular_functionS-adenosyl-L-methionine binding
B0005515molecular_functionprotein binding
B0005542molecular_functionfolic acid binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005977biological_processglycogen metabolic process
B0006111biological_processregulation of gluconeogenesis
B0006555biological_processmethionine metabolic process
B0006730biological_processone-carbon metabolic process
B0008168molecular_functionmethyltransferase activity
B0016594molecular_functionglycine binding
B0017174molecular_functionglycine N-methyltransferase activity
B0032259biological_processmethylation
B0036211biological_processprotein modification process
B0042802molecular_functionidentical protein binding
B0046498biological_processS-adenosylhomocysteine metabolic process
B0046500biological_processS-adenosylmethionine metabolic process
B0051289biological_processprotein homotetramerization
B1901052biological_processsarcosine metabolic process
B1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 1187
ChainResidue
AGLN54
AGLY186
ACYS187
AVAL204
ATHR206
AASN212

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT A 1001
ChainResidue
AHIS144
AASN193
ATYR244
ATYR285
BGLU15
ATYR33
AGLY139
AASN140

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BME B 2187
ChainResidue
BARG53
BGLN54
BGLY56
BGLY186
BCYS187
BVAL204
BTHR206
BASN212

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME B 2264
ChainResidue
BGLN257
BCYS264
BGLN265
BHIS266

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME B 2284
ChainResidue
BLYS192
BCYS284

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT B 2001
ChainResidue
BTYR33
BGLY139
BASN140
BHIS144
BASN193
BTYR222
BTYR244
BTYR285
BHOH2286
BHOH2320

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13255
ChainResidueDetails
AVAL4
AGLY139
AASN178
AMET217
ATHR223
ALEU242
BVAL4
BARG6
BALA22
BGLN31
BILE34
AARG6
BTHR41
BCYS65
BALA86
BTRP117
BGLY139
BASN178
BMET217
BTHR223
BLEU242
AALA22
AGLN31
AILE34
ATHR41
ACYS65
AALA86
ATRP117

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P13255
ChainResidueDetails
AASP2
BASP2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QXF8
ChainResidueDetails
ALEU10
BLEU10

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXF8
ChainResidueDetails
AILE34
BILE34

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXF8
ChainResidueDetails
AALA46
AASN193
ASER198
AASP203
BALA46
BASN193
BSER198
BASP203

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

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PDB entries from 2024-07-24

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