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5H9U

Crystal structure of a thermostable methionine adenosyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004478molecular_functionmethionine adenosyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006556biological_processS-adenosylmethionine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004478molecular_functionmethionine adenosyltransferase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006556biological_processS-adenosylmethionine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004478molecular_functionmethionine adenosyltransferase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006556biological_processS-adenosylmethionine biosynthetic process
C0006730biological_processone-carbon metabolic process
C0016740molecular_functiontransferase activity
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0004478molecular_functionmethionine adenosyltransferase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006556biological_processS-adenosylmethionine biosynthetic process
D0006730biological_processone-carbon metabolic process
D0016740molecular_functiontransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00376
Number of Residues11
DetailsADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY
ChainResidueDetails
CGLY127-TYR137

site_idPS00377
Number of Residues9
DetailsADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD
ChainResidueDetails
CGLY271-ASP279

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00086
ChainResidueDetails
CHIS16
AGLN100
AASP175
AARG242
AARG257
ALYS282
BHIS16
BGLU57
BGLN100
BASP175
BARG242
CGLU57
BARG257
BLYS282
DHIS16
DGLU57
DGLN100
DASP175
DARG242
DARG257
DLYS282
CGLN100
CASP175
CARG242
CARG257
CLYS282
AHIS16
AGLU57

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086
ChainResidueDetails
CASP18
ALYS278
BASP18
BGLU44
BASP251
BALA274
BLYS278
DASP18
DGLU44
DASP251
DALA274
CGLU44
DLYS278
CASP251
CALA274
CLYS278
AASP18
AGLU44
AASP251
AALA274

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PDB entries from 2024-07-10

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