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1A7A

STRUCTURE OF HUMAN PLACENTAL S-ADENOSYLHOMOCYSTEINE HYDROLASE: DETERMINATION OF A 30 SELENIUM ATOM SUBSTRUCTURE FROM DATA AT A SINGLE WAVELENGTH

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 433
ChainResidue
ATHR157
AGLU243
AILE244
AASP245
AASN248
ATHR275
ATHR276
ACYS278
AILE281
AILE299
AGLY300
ATHR158
AHIS301
AASN346
AHIS353
AADC435
AHOH459
BGLN413
BLYS426
BTYR430
ATHR159
AASP190
AASN191
AGLY220
AGLY222
AASP223
AVAL224

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD B 434
ChainResidue
AGLN413
ALYS426
ATYR430
BTHR157
BTHR158
BTHR159
BASN191
BGLY220
BGLY222
BASP223
BVAL224
BGLU243
BILE244
BASP245
BASN248
BTHR275
BTHR276
BCYS278
BILE281
BILE299
BGLY300
BHIS301
BASN346
BHIS353
BADC436
BHOH440

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ADC A 435
ChainResidue
ALEU54
AHIS55
ATHR57
AGLU59
ATHR60
AGLU156
ATHR157
ALYS186
AASP190
ALEU347
AMSE351
AHIS353
AMSE358
ANAD433
AHOH436

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADC B 436
ChainResidue
BHIS55
BTHR57
BGLU59
BTHR60
BGLU156
BTHR157
BLYS186
BASP190
BMSE351
BHIS353
BMSE358
BNAD434
BHOH454

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: 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

Catalytic Information from CSA
site_idCSA1
Number of Residues7
DetailsAnnotated By Reference To The Literature 1b3r
ChainResidueDetails
ACYS195
ALYS186
AASP131
AASN191
AHIS55
AASP190
AHIS301

site_idCSA2
Number of Residues7
DetailsAnnotated By Reference To The Literature 1b3r
ChainResidueDetails
BCYS195
BLYS186
BASP131
BASN191
BHIS55
BASP190
BHIS301

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PDB entries from 2024-08-07

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