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1O93

Methionine Adenosyltransferase complexed with ATP and a L-methionine analogue

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004478molecular_functionmethionine adenosyltransferase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006556biological_processS-adenosylmethionine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0009087biological_processL-methionine catabolic process
A0016363cellular_componentnuclear matrix
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
A0043531molecular_functionADP binding
A0046872molecular_functionmetal ion binding
A0048269cellular_componentmethionine adenosyltransferase complex
A0051289biological_processprotein homotetramerization
A0065003biological_processprotein-containing complex assembly
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004478molecular_functionmethionine adenosyltransferase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006556biological_processS-adenosylmethionine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0009087biological_processL-methionine catabolic process
B0016363cellular_componentnuclear matrix
B0016597molecular_functionamino acid binding
B0016740molecular_functiontransferase activity
B0042802molecular_functionidentical protein binding
B0043531molecular_functionADP binding
B0046872molecular_functionmetal ion binding
B0048269cellular_componentmethionine adenosyltransferase complex
B0051289biological_processprotein homotetramerization
B0065003biological_processprotein-containing complex assembly
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A1400
ChainResidue
ALYS182
AVAL205
ASER207
AMG1401

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A1401
ChainResidue
ASER248
APO41400
BASP135

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A1402
ChainResidue
BATP1397
ALYS182
ALIS1398

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A1403
ChainResidue
AGLU24
ALYS266
AHOH2001
BATP1397

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE K A1404
ChainResidue
AGLY264
AILE267
BARG265

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B1399
ChainResidue
AARG265
ALYS266
AHOH2003
BGLY280
BALA282
BLYS286

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K B1405
ChainResidue
BSER284

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LIS A1398
ChainResidue
AARG250
APHE251
AMG1402
BATP1397

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP B1397
ChainResidue
AHIS30
APRO31
AASP180
ALYS182
AGLY258
AASP259
ALYS266
ALIS1398
AMG1402
AMG1403
BALA56
BGLU71
BLYS290
BHOH2013

Functional Information from PROSITE/UniProt
site_idPS00376
Number of Residues11
DetailsADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY
ChainResidueDetails
AGLY132-TYR142

site_idPS00377
Number of Residues9
DetailsADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD
ChainResidueDetails
AGLY279-ASP287

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12888348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O93","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"description":"in other chain","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":"12888348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"10873471","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12888348","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1QM4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12888348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12888348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1fug
ChainResidueDetails
ALYS266
AHIS30
ALYS182
AARG265
BLYS286
BASP292
BLYS290

site_idCSA2
Number of Residues7
DetailsAnnotated By Reference To The Literature 1fug
ChainResidueDetails
ALYS286
AASP292
ALYS290
BLYS266
BHIS30
BLYS182
BARG265

243531

PDB entries from 2025-10-22

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