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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9QPP

CryoEM structure of human MATa2 in complex with MAT2B isoform v1 at 2.6 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004478molecular_functionmethionine adenosyltransferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006556biological_processS-adenosylmethionine biosynthetic process
A0034214biological_processprotein hexamerization
A0036094molecular_functionsmall molecule binding
A0042802molecular_functionidentical protein binding
A0048269cellular_componentmethionine adenosyltransferase complex
A0051259biological_processprotein complex oligomerization
A0051291biological_processprotein heterooligomerization
A0061431biological_processcellular response to methionine
A1904263biological_processpositive regulation of TORC1 signaling
B0004478molecular_functionmethionine adenosyltransferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005829cellular_componentcytosol
B0006556biological_processS-adenosylmethionine biosynthetic process
B0034214biological_processprotein hexamerization
B0036094molecular_functionsmall molecule binding
B0042802molecular_functionidentical protein binding
B0048269cellular_componentmethionine adenosyltransferase complex
B0051259biological_processprotein complex oligomerization
B0051291biological_processprotein heterooligomerization
B0061431biological_processcellular response to methionine
B1904263biological_processpositive regulation of TORC1 signaling
C0004478molecular_functionmethionine adenosyltransferase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005829cellular_componentcytosol
C0006556biological_processS-adenosylmethionine biosynthetic process
C0034214biological_processprotein hexamerization
C0036094molecular_functionsmall molecule binding
C0042802molecular_functionidentical protein binding
C0048269cellular_componentmethionine adenosyltransferase complex
C0051259biological_processprotein complex oligomerization
C0051291biological_processprotein heterooligomerization
C0061431biological_processcellular response to methionine
C1904263biological_processpositive regulation of TORC1 signaling
D0004478molecular_functionmethionine adenosyltransferase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005829cellular_componentcytosol
D0006556biological_processS-adenosylmethionine biosynthetic process
D0034214biological_processprotein hexamerization
D0036094molecular_functionsmall molecule binding
D0042802molecular_functionidentical protein binding
D0048269cellular_componentmethionine adenosyltransferase complex
D0051259biological_processprotein complex oligomerization
D0051291biological_processprotein heterooligomerization
D0061431biological_processcellular response to methionine
D1904263biological_processpositive regulation of TORC1 signaling
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005829cellular_componentcytosol
E0006556biological_processS-adenosylmethionine biosynthetic process
E0019899molecular_functionenzyme binding
E0030234molecular_functionenzyme regulator activity
E0048269cellular_componentmethionine adenosyltransferase complex
E0070062cellular_componentextracellular exosome
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005829cellular_componentcytosol
F0006556biological_processS-adenosylmethionine biosynthetic process
F0019899molecular_functionenzyme binding
F0030234molecular_functionenzyme regulator activity
F0048269cellular_componentmethionine adenosyltransferase complex
F0070062cellular_componentextracellular exosome
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005829cellular_componentcytosol
G0006556biological_processS-adenosylmethionine biosynthetic process
G0019899molecular_functionenzyme binding
G0030234molecular_functionenzyme regulator activity
G0048269cellular_componentmethionine adenosyltransferase complex
G0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00376
Number of Residues11
DetailsADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY
ChainResidueDetails
BGLY131-TYR141
site_idPS00377
Number of Residues9
DetailsADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD
ChainResidueDetails
BGLY278-ASP286
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsRegion: {"description":"Flexible loop","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A19","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues12
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5A1I","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26858410","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues12
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues15
DetailsRegion: {"description":"Required for interaction with MAT2A","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PDB","id":"2YDX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues14
DetailsM-CSA 9
ChainResidueDetails
AHIS29proton acceptor, proton donor
AARG264electrostatic stabiliser
ALYS265electrostatic stabiliser
ALYS285electrostatic stabiliser
ALYS289electrostatic stabiliser
AASP291electrostatic stabiliser
AASP31electrostatic stabiliser, metal ligand
ALYS32electrostatic stabiliser
AGLU57metal ligand
AGLU70electrostatic stabiliser, steric role
ALYS181electrostatic stabiliser
APHE250steric role
AASP258electrostatic stabiliser, metal ligand, steric role
AALA259metal ligand
site_idMCSA2
Number of Residues14
DetailsM-CSA 9
ChainResidueDetails
CHIS29proton acceptor, proton donor
CARG264electrostatic stabiliser
CLYS265electrostatic stabiliser
CLYS285electrostatic stabiliser
CLYS289electrostatic stabiliser
CASP291electrostatic stabiliser
CASP31electrostatic stabiliser, metal ligand
CLYS32electrostatic stabiliser
CGLU57metal ligand
CGLU70electrostatic stabiliser, steric role
CLYS181electrostatic stabiliser
CPHE250steric role
CASP258electrostatic stabiliser, metal ligand, steric role
CALA259metal ligand
site_idMCSA3
Number of Residues14
DetailsM-CSA 9
ChainResidueDetails
DHIS29proton acceptor, proton donor
DARG264electrostatic stabiliser
DLYS265electrostatic stabiliser
DLYS285electrostatic stabiliser
DLYS289electrostatic stabiliser
DASP291electrostatic stabiliser
DASP31electrostatic stabiliser, metal ligand
DLYS32electrostatic stabiliser
DGLU57metal ligand
DGLU70electrostatic stabiliser, steric role
DLYS181electrostatic stabiliser
DPHE250steric role
DASP258electrostatic stabiliser, metal ligand, steric role
DALA259metal ligand
site_idMCSA4
Number of Residues14
DetailsM-CSA 9
ChainResidueDetails
EARG29proton acceptor, proton donor
EALA264electrostatic stabiliser
EILE265electrostatic stabiliser
ELEU285electrostatic stabiliser
EARG289electrostatic stabiliser
EARG291electrostatic stabiliser
EVAL31electrostatic stabiliser, metal ligand
ELEU32electrostatic stabiliser
EGLY57metal ligand
EVAL70electrostatic stabiliser, steric role
EARG181electrostatic stabiliser
ETRP250steric role
ELYS258electrostatic stabiliser, metal ligand, steric role
ETYR259metal ligand

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PDB entries from 2026-05-27

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