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1QM4

Methionine Adenosyltransferase Complexed with 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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 398
ChainResidue
AARG265
ALYS266
BGLY280
BGLY281
BALA282
BLYS286
BK402
BHOH507

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 399
ChainResidue
AGLN184
BASP135
BGLN136
AMG405
ALYS182

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 400
ChainResidue
AGLY280
AGLY281
AALA282
ALYS286
BARG265
BLYS266
AK407

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 401
ChainResidue
APRO31
AASP180
AAMB401

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 402
ChainResidue
ASER248
BASP135
ASO4402

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K C 403
ChainResidue
AGLY264
BARG265

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K C 404
ChainResidue
BSO4401

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE K C 405
ChainResidue
ASO4403

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE AMB C 397
ChainResidue
AASP180
APHE251
AMG404

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

249697

PDB entries from 2026-02-25

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