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6SW6

Crystal structure R264H mutant of the human S-adenosylmethionine synthetase 1

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
B0004478molecular_functionmethionine adenosyltransferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006556biological_processS-adenosylmethionine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0009087biological_processmethionine catabolic process
B0016740molecular_functiontransferase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0048269cellular_componentmethionine adenosyltransferase complex
B0051289biological_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 Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13444
ChainResidueDetails
AGLU23
BGLU23

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: in other chain => ECO:0000305|PubMed:23425511, ECO:0007744|PDB:2OBV
ChainResidueDetails
AHIS29
AASP179
ASER247
BHIS29
BASP179
BSER247

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A817
ChainResidueDetails
AGLU57
AASP258
AALA281
ALYS285
BGLU57
BASP258
BALA281
BLYS285

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:P0A817
ChainResidueDetails
AGLU70
AGLN113
AHIS264
ALYS289
BGLU70
BGLN113
BHIS264
BLYS289

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P13444
ChainResidueDetails
ACYS120
BCYS120

223790

PDB entries from 2024-08-14

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