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4PGF

The structure of mono-acetylated SAHH

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 Residues27
Detailsbinding site for residue NAD A 501
ChainResidue
ATHR157
AGLU243
AILE244
AASP245
AASN248
ATHR275
ATHR276
AGLY277
AILE281
AILE299
AGLY300
ATHR158
AHIS301
AASN346
AHIS353
AGLN413
ALYS426
ATYR430
AADN502
AHOH606
ATHR159
AASN191
AGLY220
AGLY222
AASP223
AVAL224
ATHR242

site_idAC2
Number of Residues15
Detailsbinding site for residue ADN A 502
ChainResidue
AHIS55
ATHR57
AGLU59
ATHR60
AGLU156
ATHR157
ALYS186
AASP190
AHIS301
ALEU344
AMET351
AHIS353
AMET358
APHE362
ANAD501

site_idAC3
Number of Residues25
Detailsbinding site for residue NAD B 501
ChainResidue
BTHR157
BTHR158
BTHR159
BASN191
BGLY220
BGLY222
BASP223
BVAL224
BTHR242
BGLU243
BILE244
BASN248
BTHR275
BTHR276
BGLY277
BCYS278
BILE281
BILE299
BGLY300
BHIS301
BASN346
BHIS353
BLYS426
BTYR430
BADN502

site_idAC4
Number of Residues14
Detailsbinding site for residue ADN B 502
ChainResidue
BHIS55
BTHR57
BGLU59
BTHR60
BASP131
BGLU156
BTHR157
BLYS186
BASP190
BHIS301
BMET351
BHIS353
BMET358
BNAD501

Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQNhAAAAI
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 site: {"evidences":[{"source":"UniProtKB","id":"P10760","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12590576","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586999","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P50247","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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