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8P4H

Crystal structure of human methionine adenosyltransferase 2A (MAT2A) in complex with SAM and allosteric compound IDEAYA cmpd A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004478molecular_functionmethionine adenosyltransferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006556biological_processS-adenosylmethionine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0016740molecular_functiontransferase activity
A0031503biological_processprotein-containing complex localization
A0031669biological_processcellular response to nutrient levels
A0034198biological_processcellular response to amino acid starvation
A0034214biological_processprotein hexamerization
A0036094molecular_functionsmall molecule binding
A0038202biological_processTORC1 signaling
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0048269cellular_componentmethionine adenosyltransferase complex
A0051259biological_processprotein complex oligomerization
A0051291biological_processprotein heterooligomerization
A0061431biological_processcellular response to methionine
A0061462biological_processprotein localization to lysosome
A1904262biological_processnegative regulation of TORC1 signaling
A1904263biological_processpositive regulation of TORC1 signaling
A1990830biological_processcellular response to leukemia inhibitory factor
B0000166molecular_functionnucleotide binding
B0004478molecular_functionmethionine adenosyltransferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006556biological_processS-adenosylmethionine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0016740molecular_functiontransferase activity
B0031503biological_processprotein-containing complex localization
B0031669biological_processcellular response to nutrient levels
B0034198biological_processcellular response to amino acid starvation
B0034214biological_processprotein hexamerization
B0036094molecular_functionsmall molecule binding
B0038202biological_processTORC1 signaling
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0048269cellular_componentmethionine adenosyltransferase complex
B0051259biological_processprotein complex oligomerization
B0051291biological_processprotein heterooligomerization
B0061431biological_processcellular response to methionine
B0061462biological_processprotein localization to lysosome
B1904262biological_processnegative regulation of TORC1 signaling
B1904263biological_processpositive regulation of TORC1 signaling
B1990830biological_processcellular response to leukemia inhibitory factor
C0000166molecular_functionnucleotide binding
C0004478molecular_functionmethionine adenosyltransferase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006556biological_processS-adenosylmethionine biosynthetic process
C0006730biological_processone-carbon metabolic process
C0016740molecular_functiontransferase activity
C0031503biological_processprotein-containing complex localization
C0031669biological_processcellular response to nutrient levels
C0034198biological_processcellular response to amino acid starvation
C0034214biological_processprotein hexamerization
C0036094molecular_functionsmall molecule binding
C0038202biological_processTORC1 signaling
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0048269cellular_componentmethionine adenosyltransferase complex
C0051259biological_processprotein complex oligomerization
C0051291biological_processprotein heterooligomerization
C0061431biological_processcellular response to methionine
C0061462biological_processprotein localization to lysosome
C1904262biological_processnegative regulation of TORC1 signaling
C1904263biological_processpositive regulation of TORC1 signaling
C1990830biological_processcellular response to leukemia inhibitory factor
D0000166molecular_functionnucleotide binding
D0004478molecular_functionmethionine adenosyltransferase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0006556biological_processS-adenosylmethionine biosynthetic process
D0006730biological_processone-carbon metabolic process
D0016740molecular_functiontransferase activity
D0031503biological_processprotein-containing complex localization
D0031669biological_processcellular response to nutrient levels
D0034198biological_processcellular response to amino acid starvation
D0034214biological_processprotein hexamerization
D0036094molecular_functionsmall molecule binding
D0038202biological_processTORC1 signaling
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0048269cellular_componentmethionine adenosyltransferase complex
D0051259biological_processprotein complex oligomerization
D0051291biological_processprotein heterooligomerization
D0061431biological_processcellular response to methionine
D0061462biological_processprotein localization to lysosome
D1904262biological_processnegative regulation of TORC1 signaling
D1904263biological_processpositive regulation of TORC1 signaling
D1990830biological_processcellular response to leukemia inhibitory factor
Functional Information from PROSITE/UniProt
site_idPS00376
Number of Residues11
DetailsADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY
ChainResidueDetails
AGLY131-TYR141

site_idPS00377
Number of Residues9
DetailsADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD
ChainResidueDetails
AGLY278-ASP286

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19
ChainResidueDetails
AHIS29
AARG264
BHIS29
BARG264
CHIS29
CARG264
DHIS29
DARG264

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I
ChainResidueDetails
AASP31
BASP31
CASP31
DASP31

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A817
ChainResidueDetails
AGLU57
BGLU57
CGLU57
DGLU57

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN
ChainResidueDetails
AGLU70
BGLU70
CGLU70
DGLU70

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: in other chain => ECO:0000305|PubMed:25075345
ChainResidueDetails
AGLN113
BGLN113
CGLN113
DGLN113

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A19, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I
ChainResidueDetails
AASP179
BASP179
CASP179
DASP179

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: in other chain => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4KTT, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A1G, ECO:0007744|PDB:5A1I
ChainResidueDetails
ASER247
BSER247
CSER247
DSER247

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN, ECO:0007744|PDB:5A1I
ChainResidueDetails
AASP258
BASP258
CASP258
DASP258

site_idSWS_FT_FI9
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0007744|PDB:4NDN
ChainResidueDetails
AALA281
BALA281
CALA281
DALA281

site_idSWS_FT_FI10
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:25075345, ECO:0000305|PubMed:26858410, ECO:0007744|PDB:4NDN
ChainResidueDetails
ALYS285
AASP291
BLYS285
BASP291
CLYS285
CASP291
DLYS285
DASP291

site_idSWS_FT_FI11
Number of Residues4
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P0A817
ChainResidueDetails
ALYS289
BLYS289
CLYS289
DLYS289

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS81
BLYS81
CLYS81
DLYS81

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER114
BSER114
CSER114
DSER114

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER384
BSER384
CSER384
DSER384

site_idSWS_FT_FI15
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS228
DLYS228
DLYS234
ALYS234
BLYS228
BLYS234
CLYS228
CLYS234

Catalytic Information from CSA
site_idMCSA1
Number of Residues14
DetailsM-CSA 9
ChainResidueDetails
AHIS29proton acceptor, proton donor
AVAL268electrostatic stabiliser
AASP269electrostatic stabiliser
ALYS289electrostatic stabiliser
ASER293electrostatic stabiliser
AALA295electrostatic stabiliser
AASP31electrostatic stabiliser, metal ligand
ALYS32electrostatic stabiliser
AGLU57metal ligand
AGLU70electrostatic stabiliser, steric role
ALYS181electrostatic stabiliser
AGLY254steric role
ATHR262electrostatic stabiliser, metal ligand, steric role
AGLY263metal ligand

site_idMCSA2
Number of Residues14
DetailsM-CSA 9
ChainResidueDetails
BHIS29proton acceptor, proton donor
BVAL268electrostatic stabiliser
BASP269electrostatic stabiliser
BLYS289electrostatic stabiliser
BSER293electrostatic stabiliser
BALA295electrostatic stabiliser
BASP31electrostatic stabiliser, metal ligand
BLYS32electrostatic stabiliser
BGLU57metal ligand
BGLU70electrostatic stabiliser, steric role
BLYS181electrostatic stabiliser
BGLY254steric role
BTHR262electrostatic stabiliser, metal ligand, steric role
BGLY263metal ligand

site_idMCSA3
Number of Residues14
DetailsM-CSA 9
ChainResidueDetails
CHIS29proton acceptor, proton donor
CVAL268electrostatic stabiliser
CASP269electrostatic stabiliser
CLYS289electrostatic stabiliser
CSER293electrostatic stabiliser
CALA295electrostatic stabiliser
CASP31electrostatic stabiliser, metal ligand
CLYS32electrostatic stabiliser
CGLU57metal ligand
CGLU70electrostatic stabiliser, steric role
CLYS181electrostatic stabiliser
CGLY254steric role
CTHR262electrostatic stabiliser, metal ligand, steric role
CGLY263metal ligand

site_idMCSA4
Number of Residues14
DetailsM-CSA 9
ChainResidueDetails
DHIS29proton acceptor, proton donor
DVAL268electrostatic stabiliser
DASP269electrostatic stabiliser
DLYS289electrostatic stabiliser
DSER293electrostatic stabiliser
DALA295electrostatic stabiliser
DASP31electrostatic stabiliser, metal ligand
DLYS32electrostatic stabiliser
DGLU57metal ligand
DGLU70electrostatic stabiliser, steric role
DLYS181electrostatic stabiliser
DGLY254steric role
DTHR262electrostatic stabiliser, metal ligand, steric role
DGLY263metal ligand

237992

PDB entries from 2025-06-25

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