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5T8S

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

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 401
ChainResidue
AASP276
AHOH535
AHOH543
B3PO404
BHOH557
BHOH578

site_idAC2
Number of Residues16
Detailsbinding site for residue AMP A 402
ChainResidue
ALYS168
ASER191
ATHR232
AARG234
APHE235
AASP243
APOP404
AHOH502
AHOH668
AHOH699
BGLY120
BASP121
BHOH650
AHIS15
APRO16
AASP166

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 403
ChainResidue
AASP17
ALYS250
APOP404
APO4405
AHOH524
AHOH656

site_idAC4
Number of Residues21
Detailsbinding site for residue POP A 404
ChainResidue
AHIS15
AASP17
ALYS168
ALYS250
AAMP402
AMG403
APO4405
AHOH524
AHOH541
AHOH596
AHOH652
AHOH656
AHOH683
AHOH692
AHOH736
BASP121
BLYS270
BASP276
BMG403
BHOH595
BHOH600

site_idAC5
Number of Residues14
Detailsbinding site for residue PO4 A 405
ChainResidue
AASP17
AARG249
ALYS250
AMG403
APOP404
AHOH524
AHOH659
AHOH736
BGLY264
BGLY265
BALA266
BLYS270
BASP276
BMG403

site_idAC6
Number of Residues5
Detailsbinding site for residue MG B 401
ChainResidue
BASP17
BLYS250
B3PO404
BHOH528
BHOH583

site_idAC7
Number of Residues25
Detailsbinding site for residue SAM B 402
ChainResidue
AALA41
AGLU56
AGLN99
AASP102
AILE103
AGLY120
AASP121
ALYS274
AILE307
AHOH585
AHOH732
BHIS15
BPRO16
BASP166
BLYS168
BSER191
BARG234
BPHE235
BASP243
B3PO404
BHOH535
BHOH577
BHOH602
BHOH620
BHOH638

site_idAC8
Number of Residues5
Detailsbinding site for residue MG B 403
ChainResidue
APOP404
APO4405
AHOH736
BASP276
BHOH600

site_idAC9
Number of Residues21
Detailsbinding site for residue 3PO B 404
ChainResidue
AGLY265
AALA266
ALYS270
AASP276
AMG401
AHOH543
BHIS15
BASP17
BLYS168
BARG249
BLYS250
BMG401
BSAM402
BHOH523
BHOH528
BHOH535
BHOH551
BHOH557
BHOH583
BHOH618
AASP121

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 2024-08-07

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