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2OBV

Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product

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
A0009087biological_processL-methionine catabolic process
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0048269cellular_componentmethionine adenosyltransferase complex
A0051259biological_processprotein complex oligomerization
A0051289biological_processprotein homotetramerization
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 401
ChainResidue
AASP166

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 402
ChainResidue
AGLU147
AGLU216
ALYS307

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE SAM A 501
ChainResidue
AASP116
AILE117
AGLY133
AASP134
AASP179
ALYS181
ASER247
AARG249
APHE250
AASP258
ALYS289
AHOH644
AHOH652
AHOH687
AHOH732
AHOH753
AHOH798
AHIS29
APRO30
AALA55
AGLU70
AGLN113

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG4 A 601
ChainResidue
AGLN190
AGLY193
AARG313

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 602
ChainResidue
AGLU148
ALYS159
ATYR377
AARG382

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PG4 A 603
ChainResidue
ATHR146
AGLU147
AGLU211
AASP212
AILE213
ALYS307
AHOH738

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 Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P13444","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"23425511","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2OBV","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":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P13444","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fug
ChainResidueDetails
AASP291
ALYS285
ALYS289

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1fug
ChainResidueDetails
AARG264
ALYS181
ALYS265
AHIS29

239149

PDB entries from 2025-07-23

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