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2AZT

Crystal structure of H176N mutant 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
A0016740molecular_functiontransferase activity
A0017174molecular_functionglycine N-methyltransferase activity
A0032259biological_processmethylation
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
B0016740molecular_functiontransferase activity
B0017174molecular_functionglycine N-methyltransferase activity
B0032259biological_processmethylation
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 Residues2
DetailsBINDING SITE FOR RESIDUE CL B 3000
ChainResidue
BGLN58
BPHE79

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 1188
ChainResidue
ACYS187
AALA188
APRO189
AVAL204
ATHR206
AASN212

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A 1285
ChainResidue
ACYS284
AILE282

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BME B 2188
ChainResidue
BARG53
BGLN54
BGLY186
BCYS187
BPRO189
BVAL204
BTHR206
BASN212

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME B 2249
ChainResidue
BLEU183
BCYS248

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME B 2285
ChainResidue
BHIS181
BLYS192
BILE282
BCYS284

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT A 1000
ChainResidue
ATYR33
AGLY139
AASN140
AHIS144
AARG177
AASN193
ATYR222
ATYR244
ATYR285
BGLU15

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT B 2000
ChainResidue
AGLU15
BTYR33
BGLY139
BASN140
BHIS144
BASN193
BTYR222
BTYR244
BTYR285

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P13255","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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 2025-10-15

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