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3GLQ

Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei in complex with 9-beta-D-arabino-furansyl-adenine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004013molecular_functionadenosylhomocysteinase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016787molecular_functionhydrolase activity
A0033353biological_processS-adenosylmethionine cycle
B0004013molecular_functionadenosylhomocysteinase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0016787molecular_functionhydrolase activity
B0033353biological_processS-adenosylmethionine cycle
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NAD A 601
ChainResidue
ATHR200
AGLU286
AILE287
AASP288
ACYS291
AALA318
ATHR319
AGLY320
AASN321
AILE342
AGLY343
ATHR201
AHIS344
ALEU385
AASN387
AHIS394
AHOH503
AHOH532
AHOH557
ARAB602
AHOH628
AHOH741
ATHR202
BGLN454
BLYS467
BTYR471
AASN234
AGLY263
AGLY265
AASP266
AVAL267
ATHR285

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE RAB A 602
ChainResidue
ALEU61
AHIS62
ATHR64
AGLN66
ATHR67
AASP139
AGLU199
ATHR200
ALYS229
AASP233
AHIS344
ALEU385
ATHR392
AHIS394
AMET399
APHE403
ANAD601

site_idAC3
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NAD B 601
ChainResidue
AGLN454
ALYS467
ATYR471
BTHR200
BTHR201
BTHR202
BASN234
BGLY263
BGLY265
BASP266
BVAL267
BTHR285
BGLU286
BILE287
BASP288
BCYS291
BALA318
BTHR319
BGLY320
BASN321
BVAL324
BILE342
BGLY343
BHIS344
BLEU385
BASN387
BHIS394
BHOH503
BHOH541
BHOH573
BRAB602
BHOH623
BHOH694
BHOH778

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE RAB B 602
ChainResidue
BPHE403
BNAD601
BLEU61
BHIS62
BTHR64
BGLN66
BTHR67
BASP139
BTHR200
BLYS229
BASP233
BHIS344
BLEU385
BLEU388
BTHR392
BGLY393
BHIS394
BMET399

Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDhAAAAI
ChainResidueDetails
ASER85-ILE99

site_idPS00739
Number of Residues17
DetailsADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKiavVaGYGdVGKGc.A
ChainResidueDetails
AGLY256-ALA272

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING:
ChainResidueDetails
BASP139
BGLU199
BLYS229
BASP233
ATHR64
AASP139
AGLU199
ALYS229
AASP233
BTHR64

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563
ChainResidueDetails
BASN234
BGLY263
ATHR200
AASN234
AGLY263
BTHR200

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563, ECO:0000269|Ref.2, ECO:0000269|Ref.3
ChainResidueDetails
AASP266
AGLU286
AASN321
AILE342
AASN387
BASP266
BGLU286
BASN321
BILE342
BASN387

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PDB entries from 2024-06-12

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