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7BHU

Crystal structure of MAT2a with elaborated fragment 26 bound in the allosteric site

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
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue TOW A 401
ChainResidue
APHE18
APHE333
ATYR335
AEDO403
AEDO403
AHOH579
APHE20
APHE139
AGLN190
AGLY273
ATRP274
AGLY275
AARG313
AGLN317

site_idAC2
Number of Residues21
Detailsbinding site for residue SAM A 402
ChainResidue
AHIS29
APRO30
AALA55
AGLU70
AGLN113
AASP116
AILE117
AGLY133
AASP134
AASP179
ALYS181
ASER247
AARG249
APHE250
AASP258
ALYS289
AHOH552
AHOH592
AHOH639
AHOH640
AHOH703

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 403
ChainResidue
AGLY275
AGLY275
ATYR335
ATYR335
ATOW401
ATOW401

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 Residues12
DetailsRegion: {"description":"Flexible loop","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
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 Residues1
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 Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
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 Residues1
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
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 Residues3
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 Residues1
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 Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25075345","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NDN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
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 Residues1
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","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

238582

PDB entries from 2025-07-09

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