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5M65

Crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with 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 Residues31
Detailsbinding site for residue NAD A 501
ChainResidue
ATHR198
AVAL285
AASP286
ATHR317
AGLY318
AASN319
AILE322
AILE340
AGLY341
AHIS342
ALEU383
ATHR199
AASN385
AHIS392
AADE502
AHOH678
AHOH680
AHOH696
AHOH709
AHOH737
AHOH743
BGLN454
ATHR200
BLYS467
BTYR471
AASN232
AGLY263
AASP264
AVAL265
ASER283
AGLU284

site_idAC2
Number of Residues10
Detailsbinding site for residue ADE A 502
ChainResidue
AHIS58
ATHR60
AGLN62
ATHR63
AMET390
AGLY391
AHIS392
AMET397
ANAD501
AHOH753

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 503
ChainResidue
AGLN62
AMET390
AHIS392
AHOH650
AHOH671
AHOH797

site_idAC4
Number of Residues1
Detailsbinding site for residue BR A 504
ChainResidue
AASP371

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 505
ChainResidue
AMET251
ASER253
ALYS255
ALYS442
AHOH673

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO A 506
ChainResidue
ASER468
AHIS470
ATYR471
AHOH620
AHOH764
AHOH803
BASP223

site_idAC7
Number of Residues30
Detailsbinding site for residue NAD B 501
ChainResidue
ALYS467
ATYR471
BTHR198
BTHR199
BTHR200
BASN232
BGLY263
BASP264
BVAL265
BGLU284
BVAL285
BASP286
BCYS289
BTHR317
BGLY318
BASN319
BILE322
BILE340
BGLY341
BHIS342
BLEU383
BASN385
BHIS392
BADE502
BHOH645
BHOH679
BHOH687
BHOH737
BHOH749
BHOH780

site_idAC8
Number of Residues10
Detailsbinding site for residue ADE B 502
ChainResidue
BNAD501
BLEU57
BHIS58
BTHR60
BGLN62
BTHR63
BMET390
BGLY391
BHIS392
BMET397

site_idAC9
Number of Residues6
Detailsbinding site for residue NA B 503
ChainResidue
BGLN62
BMET390
BHIS392
BHOH640
BHOH801
BHOH804

site_idAD1
Number of Residues2
Detailsbinding site for residue BR B 504
ChainResidue
ALYS189
BASP371

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO B 505
ChainResidue
BTHR200
BHIS203
BGLY318
BHOH601

site_idAD3
Number of Residues7
Detailsbinding site for residue EDO B 506
ChainResidue
BMET251
BSER253
BLYS255
BPHE395
BLYS442
BILE443
BHOH733

site_idAD4
Number of Residues4
Detailsbinding site for residue EDO B 507
ChainResidue
BPHE20
BLYS23
BILE360
BLYS361

Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiYSTQDhAAAAI
ChainResidueDetails
ASER81-ILE95

site_idPS00739
Number of Residues18
DetailsADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvamVaGFGdVGKGsaA
ChainResidueDetails
AGLY254-ALA271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:26627650
ChainResidueDetails
BHIS342
BHIS392
AHIS58
AHIS342
AHIS392
BHIS58

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563, ECO:0000305|PubMed:26627650
ChainResidueDetails
BASP135
BGLU197
BLYS227
BASP231
AASP135
AGLU197
ALYS227
AASP231

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00563, ECO:0000269|PubMed:26627650
ChainResidueDetails
BASN232
BGLU284
BILE340
BASN385
AGLU284
AILE340
AASN385
BTHR198
ATHR198
AASN232

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: in other chain => ECO:0000269|PubMed:26627650
ChainResidueDetails
AVAL265
BVAL265

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00563
ChainResidueDetails
AASN319
BASN319

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26627650
ChainResidueDetails
ALYS467
ATYR471
BLYS467
BTYR471

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PDB entries from 2024-05-15

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