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5W49

The crystal structure of human S-adenosylhomocysteine hydrolase (AHCY) bound to oxadiazole inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004013molecular_functionadenosylhomocysteinase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016787molecular_functionhydrolase activity
A0033353biological_processS-adenosylmethionine cycle
A0042470cellular_componentmelanosome
A0070062cellular_componentextracellular exosome
B0004013molecular_functionadenosylhomocysteinase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0016787molecular_functionhydrolase activity
B0033353biological_processS-adenosylmethionine cycle
B0042470cellular_componentmelanosome
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue NAD A 501
ChainResidue
AASP190
AASN248
ATHR275
ATHR276
AGLY277
ACYS278
AILE281
AILE299
AGLY300
AASN346
AHOH649
AASN191
AHOH650
AHOH652
AHOH671
BGLN413
BLYS426
BTYR430
AGLY222
AASP223
AVAL224
ATHR242
AGLU243
AILE244
AASP245

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 502
ChainResidue
AARG205
ALYS322
APRO323
ACYS349
AHOH620

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 503
ChainResidue
AMET210
AALA212
ALYS214
BPHE356
BLYS401
BLEU402

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 504
ChainResidue
AGLY284
AARG285
AASP307
ATRP310

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 505
ChainResidue
APHE356
ALYS401
AHOH626
BMET210
BALA212
BLYS214

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO A 506
ChainResidue
AVAL161
AASN181
AASP182
BHIS429

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 507
ChainResidue
AASN320
AGLN324
AASP326
AGLU341

site_idAC8
Number of Residues12
Detailsbinding site for residue 9W1 A 508
ChainResidue
AHIS55
ATHR57
AGLU59
ATHR60
ASER83
AGLN85
ALEU347
AALA350
AMET351
AHIS353
AMET358
APHE362

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO A 509
ChainResidue
AGLY213
AVAL215
AARG238
ATYR257
BLEU402

site_idAD1
Number of Residues31
Detailsbinding site for residue NAD B 501
ChainResidue
BHOH725
BHOH741
BHOH744
ALEU409
AGLN413
ALYS426
ATYR430
BASP190
BASN191
BGLY222
BASP223
BVAL224
BTHR242
BGLU243
BILE244
BASP245
BASN248
BTHR275
BTHR276
BGLY277
BCYS278
BILE281
BILE299
BGLY300
BHIS301
BASN346
B9W1509
BHOH616
BHOH651
BHOH660
BHOH661

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO B 502
ChainResidue
BLEU283
BGLY284
BARG285
BASP307
BTRP310

site_idAD3
Number of Residues9
Detailsbinding site for residue EDO B 503
ChainResidue
ALEU402
AASN403
BGLY213
BVAL215
BARG238
BALA253
BTYR257
BGLU258
BHOH617

site_idAD4
Number of Residues5
Detailsbinding site for residue EDO B 504
ChainResidue
BGLU317
BVAL319
BARG327
BARG329
BHOH606

site_idAD5
Number of Residues8
Detailsbinding site for residue EDO B 505
ChainResidue
ATHR207
AASP208
AVAL209
BGLU28
BSER355
BHOH608
BHOH624
BHOH672

site_idAD6
Number of Residues5
Detailsbinding site for residue EDO B 506
ChainResidue
BTRP17
BLYS20
BVAL316
BGLU317
BARG329

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO B 507
ChainResidue
AHIS429
BVAL161
BASN181
BASP182

site_idAD8
Number of Residues4
Detailsbinding site for residue EDO B 508
ChainResidue
BARG205
BLYS322
BPRO323
BCYS349

site_idAD9
Number of Residues13
Detailsbinding site for residue 9W1 B 509
ChainResidue
BHIS55
BTHR57
BGLU59
BTHR60
BSER83
BGLN85
BLEU347
BALA350
BMET351
BHIS353
BMET358
BPHE362
BNAD501

Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDhAAAAI
ChainResidueDetails
ASER78-ILE92

site_idPS00739
Number of Residues17
DetailsADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvavVaGYGdVGKGc.A
ChainResidueDetails
AGLY213-ALA229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P10760
ChainResidueDetails
ATHR57
BASP190
AASP131
AGLU156
ALYS186
AASP190
BTHR57
BASP131
BGLU156
BLYS186

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:12590576, ECO:0000269|PubMed:9586999
ChainResidueDetails
ATHR157
BGLU243
BASN248
BILE299
BASN346
BHIS353
AGLY222
AGLU243
AASN248
AILE299
AASN346
AHIS353
BTHR157
BGLY222

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER183
BSER183

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
ChainResidueDetails
ALYS186
BLYS186

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P50247
ChainResidueDetails
ATYR193
BTYR193

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PDB entries from 2024-07-17

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