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5T8T

Crystal Structure of a S-adenosylmethionine Synthase from Neisseria gonorrhoeae with bound AMP and Magnesium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004478molecular_functionmethionine adenosyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
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
B0005829cellular_componentcytosol
B0006556biological_processS-adenosylmethionine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0016740molecular_functiontransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue AMP B 401
ChainResidue
AASP102
BSER191
BTHR232
BARG234
BPHE235
BASP243
BLYS250
BMG402
BHOH501
BHOH503
BHOH516
AILE103
BHOH558
BHOH560
BHOH643
AASP121
AHOH473
BHIS15
BPRO16
BASP17
BASP166
BLYS168

site_idAC2
Number of Residues4
Detailsbinding site for residue MG B 402
ChainResidue
BASP17
BARG249
BLYS250
BAMP401

Functional Information from PROSITE/UniProt
site_idPS00376
Number of Residues11
DetailsADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY
ChainResidueDetails
AGLY118-TYR128

site_idPS00377
Number of Residues9
DetailsADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD
ChainResidueDetails
AGLY263-ASP271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00086
ChainResidueDetails
AHIS15
BGLN99
BASP166
BARG234
BARG249
BLYS274
AGLU56
AGLN99
AASP166
AARG234
AARG249
ALYS274
BHIS15
BGLU56

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086
ChainResidueDetails
AASP17
BLYS270
AGLU43
AASP243
AALA266
ALYS270
BASP17
BGLU43
BASP243
BALA266

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PDB entries from 2024-09-11

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