Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4PFJ

The structure of bi-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 Residues31
Detailsbinding site for residue NAD A 501
ChainResidue
ATHR157
AGLU243
AILE244
AASP245
AASN248
ATHR275
ATHR276
AGLY277
ACYS278
AILE281
AILE299
ATHR158
AGLY300
AHIS301
AASN346
AHIS353
AGLN413
ALYS426
ATYR430
AADN502
AHOH658
AHOH681
ATHR159
AHOH685
AHOH699
AASN191
AGLY220
AGLY222
AASP223
AVAL224
ATHR242

site_idAC2
Number of Residues15
Detailsbinding site for residue ADN A 502
ChainResidue
AHIS55
ATHR57
AGLU59
ATHR60
AASP131
AGLU156
ATHR157
ALYS186
AASP190
AHIS301
AMET351
AHIS353
AMET358
APHE362
ANAD501

site_idAC3
Number of Residues29
Detailsbinding site for residue NAD B 501
ChainResidue
BTHR157
BTHR158
BTHR159
BASN191
BGLY222
BASP223
BVAL224
BTHR242
BGLU243
BILE244
BASP245
BASN248
BTHR275
BTHR276
BGLY277
BCYS278
BILE281
BILE299
BGLY300
BHIS301
BASN346
BHIS353
BGLN413
BLYS426
BTYR430
BADN502
BHOH657
BHOH674
BHOH682

site_idAC4
Number of Residues15
Detailsbinding site for residue ADN B 502
ChainResidue
BHIS55
BTHR57
BGLU59
BTHR60
BASP131
BGLU156
BTHR157
BLYS186
BASP190
BHIS301
BMET351
BHIS353
BMET358
BPHE362
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

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon