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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1NBI

Structure of R175K mutated glycine N-methyltransferase complexed with S-adenosylmethionine, R175K:SAM.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005542molecular_functionfolic acid binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006111biological_processregulation of gluconeogenesis
A0006544biological_processglycine metabolic process
A0006546biological_processglycine catabolic process
A0006730biological_processone-carbon metabolic process
A0016594molecular_functionglycine binding
A0017174molecular_functionglycine N-methyltransferase activity
A0018013biological_processN-terminal peptidyl-glycine methylation
A0034708cellular_componentmethyltransferase complex
A0042802molecular_functionidentical protein binding
A0046500biological_processS-adenosylmethionine metabolic process
A0050843biological_processS-adenosylmethionine catabolic process
A0051289biological_processprotein homotetramerization
A0098603molecular_functionselenol Se-methyltransferase activity
A1901052biological_processsarcosine metabolic process
A1901605biological_processalpha-amino acid metabolic process
A1904047molecular_functionS-adenosyl-L-methionine binding
B0005542molecular_functionfolic acid binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006111biological_processregulation of gluconeogenesis
B0006544biological_processglycine metabolic process
B0006546biological_processglycine catabolic process
B0006730biological_processone-carbon metabolic process
B0016594molecular_functionglycine binding
B0017174molecular_functionglycine N-methyltransferase activity
B0018013biological_processN-terminal peptidyl-glycine methylation
B0034708cellular_componentmethyltransferase complex
B0042802molecular_functionidentical protein binding
B0046500biological_processS-adenosylmethionine metabolic process
B0050843biological_processS-adenosylmethionine catabolic process
B0051289biological_processprotein homotetramerization
B0098603molecular_functionselenol Se-methyltransferase activity
B1901052biological_processsarcosine metabolic process
B1901605biological_processalpha-amino acid metabolic process
B1904047molecular_functionS-adenosyl-L-methionine binding
C0005542molecular_functionfolic acid binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006111biological_processregulation of gluconeogenesis
C0006544biological_processglycine metabolic process
C0006546biological_processglycine catabolic process
C0006730biological_processone-carbon metabolic process
C0016594molecular_functionglycine binding
C0017174molecular_functionglycine N-methyltransferase activity
C0018013biological_processN-terminal peptidyl-glycine methylation
C0034708cellular_componentmethyltransferase complex
C0042802molecular_functionidentical protein binding
C0046500biological_processS-adenosylmethionine metabolic process
C0050843biological_processS-adenosylmethionine catabolic process
C0051289biological_processprotein homotetramerization
C0098603molecular_functionselenol Se-methyltransferase activity
C1901052biological_processsarcosine metabolic process
C1901605biological_processalpha-amino acid metabolic process
C1904047molecular_functionS-adenosyl-L-methionine binding
D0005542molecular_functionfolic acid binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006111biological_processregulation of gluconeogenesis
D0006544biological_processglycine metabolic process
D0006546biological_processglycine catabolic process
D0006730biological_processone-carbon metabolic process
D0016594molecular_functionglycine binding
D0017174molecular_functionglycine N-methyltransferase activity
D0018013biological_processN-terminal peptidyl-glycine methylation
D0034708cellular_componentmethyltransferase complex
D0042802molecular_functionidentical protein binding
D0046500biological_processS-adenosylmethionine metabolic process
D0050843biological_processS-adenosylmethionine catabolic process
D0051289biological_processprotein homotetramerization
D0098603molecular_functionselenol Se-methyltransferase activity
D1901052biological_processsarcosine metabolic process
D1901605biological_processalpha-amino acid metabolic process
D1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SAM A 293
ChainResidue
ATYR21
ASER87
AMET90
AALA115
AASN116
ATRP117
ALEU136
ASER139
AHIS142
ATYR194
ATRP30
AILE34
AARG40
AALA64
AGLY66
AVAL69
AASP85
AALA86
site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE SAM B 1293
ChainResidue
BTYR21
BTRP30
BILE34
BARG40
BALA64
BGLY66
BVAL69
BASP85
BALA86
BSER87
BMET90
BALA115
BASN116
BTRP117
BLEU136
BSER139
BHIS142
BTYR194
BHOH5048
site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SAM C 2293
ChainResidue
CTYR21
CTRP30
CILE34
CARG40
CALA64
CTHR67
CASP85
CALA86
CSER87
CMET90
CALA115
CASN116
CTRP117
CLEU136
CGLY137
CSER139
CHIS142
site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE SAM D 3293
ChainResidue
DTRP30
DILE34
DARG40
DALA64
DTHR67
DASP85
DALA86
DSER87
DMET90
DALA115
DASN116
DTRP117
DLEU136
DSER139
DHIS142
DTYR194
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8810903","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XVA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8810903","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XVA","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12859184","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8810903","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NBI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XVA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22037183","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3THR","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3THS","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues16
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9QXF8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 23
ChainResidueDetails
ATYR21electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AGLY137electrostatic stabiliser, hydrogen bond acceptor
AHIS142activator
ALYS175electrostatic 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
BLYS175electrostatic stabiliser
BTYR194electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
site_idMCSA3
Number of Residues5
DetailsM-CSA 23
ChainResidueDetails
CTYR21electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
CGLY137electrostatic stabiliser, hydrogen bond acceptor
CHIS142activator
CLYS175electrostatic stabiliser
CTYR194electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
site_idMCSA4
Number of Residues5
DetailsM-CSA 23
ChainResidueDetails
DTYR21electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
DGLY137electrostatic stabiliser, hydrogen bond acceptor
DHIS142activator
DLYS175electrostatic stabiliser
DTYR194electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

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PDB entries from 2026-04-01

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