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8SWA

Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with SAM and PPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004478molecular_functionmethionine adenosyltransferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006556biological_processS-adenosylmethionine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0009087biological_processmethionine catabolic process
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0048269cellular_componentmethionine adenosyltransferase complex
A0051289biological_processprotein homotetramerization
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 Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13444
ChainResidueDetails
AGLU23

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: in other chain => ECO:0000305|PubMed:23425511, ECO:0007744|PDB:2OBV
ChainResidueDetails
AHIS29
AASP179
ASER247

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A817
ChainResidueDetails
AGLU57
AASP258
AALA281
ALYS285

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P0A817
ChainResidueDetails
AGLU70
AGLN113
AARG264
ALYS289

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P13444
ChainResidueDetails
ACYS120

221051

PDB entries from 2024-06-12

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