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4YVF

Structure of S-adenosyl-L-homocysteine hydrolase

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 Residues31
Detailsbinding site for residue NAI A 501
ChainResidue
AASP190
AASP245
AASN248
ATHR275
ATHR276
AGLY277
ACYS278
AILE281
AILE299
AGLY300
AHIS301
AASN191
ALEU344
AASN346
AHIS353
AXFA502
AHOH646
AHOH655
AHOH668
AHOH678
AHOH681
AHOH684
ACYS195
BLYS426
BTYR430
AGLY222
AASP223
AVAL224
ATHR242
AGLU243
AILE244

site_idAC2
Number of Residues15
Detailsbinding site for residue XFA A 502
ChainResidue
AHIS55
ATHR57
AGLU59
ASER83
AGLN85
AASP190
ALEU344
AASN346
ALEU347
AMET351
AGLY352
AHIS353
AMET358
ANAI501
AHOH620

site_idAC3
Number of Residues33
Detailsbinding site for residue NAI B 501
ChainResidue
ALEU409
AGLN413
ALYS426
ATYR430
BASP190
BASN191
BCYS195
BGLY222
BASP223
BVAL224
BTHR242
BGLU243
BILE244
BASP245
BASN248
BTHR275
BTHR276
BGLY277
BCYS278
BILE281
BILE299
BGLY300
BHIS301
BASN346
BHIS353
BXFA502
BHOH619
BHOH626
BHOH653
BHOH659
BHOH671
BHOH673
BHOH678

site_idAC4
Number of Residues14
Detailsbinding site for residue XFA B 502
ChainResidue
BHIS55
BTHR57
BGLU59
BSER83
BGLN85
BASP190
BLEU344
BASN346
BLEU347
BMET351
BGLY352
BHIS353
BNAI501
BHOH614

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: N-acetylserine => ECO:0000269|Ref.8
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER183
BSER183

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
ChainResidueDetails
ALYS186
BLYS186

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P50247
ChainResidueDetails
ATYR193
BTYR193

223790

PDB entries from 2024-08-14

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