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3RV2

Crystal structure of S-adenosylmethionine synthetase from Mycobacterium marinum

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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
AASP259
AHOH447
AHOH448
AHOH482
AHOH506
AHOH601

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 405
ChainResidue
AHOH454
AHOH455
AHOH478
AASP394
AASP397
AASP398

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 406
ChainResidue
AHIS158
AARG162
AGLY382
AARG383
ATHR384
AASP385
AHOH464

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 407
ChainResidue
AARG41
AALA43
AGLU58
AVAL59
ATHR60
ALYS290

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BASP259
BHOH442
BHOH466
BHOH490
BHOH545
BHOH604
BHOH611

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 405
ChainResidue
BHIS158
BARG162
BGLY382
BARG383
BTHR384
BASP385
BHOH535

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 406
ChainResidue
AARG363
AASP364
BASP364
BASP394
BLYS395

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 407
ChainResidue
AASP364
AASP394
ALYS395
BARG363
BASP364

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 408
ChainResidue
BARG41
BVAL42
BALA43
BGLU58
BVAL59
BTHR60
BLYS290
BHOH485

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
AGLY279-ASP287

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00086
ChainResidueDetails
AHIS17
BGLN104
BASP179
BLYS250
BARG265
BLYS290
AGLU58
AGLN104
AASP179
ALYS250
AARG265
ALYS290
BHIS17
BGLU58

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086
ChainResidueDetails
AASP19
BLYS286
AGLU45
AASP259
AALA282
ALYS286
BASP19
BGLU45
BASP259
BALA282

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PDB entries from 2024-09-04

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