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1LI4

Human S-adenosylhomocysteine hydrolase complexed with neplanocin

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
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NAD A 433
ChainResidue
ATHR157
ATHR242
AGLU243
AILE244
AASP245
AASN248
ATHR275
ATHR276
ACYS278
AILE281
AILE299
ATHR158
AGLY300
AHIS301
ALEU344
AASN346
AHIS353
ALYS426
ATYR430
ANOC434
AHOH903
AHOH929
ATHR159
AHOH930
AHOH938
AHOH998
AASP190
AASN191
AGLY220
AGLY222
AASP223
AVAL224

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NOC A 434
ChainResidue
AHIS55
ATHR57
AGLU59
ATHR60
AASP131
AGLU156
ATHR157
ALYS186
AASP190
AHIS301
AMET351
AGLY352
AHIS353
AMET358
APHE362
ANAD433

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA A 900
ChainResidue
AARG238
AALA253
ATYR257
AVAL259
ALEU402
AHOH1039

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA A 901
ChainResidue
AGLN85
AASP86
AHIS87

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 Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P10760
ChainResidueDetails
ATHR57
AASP131
AGLU156
ALYS186
AASP190

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:12590576, ECO:0000269|PubMed:9586999
ChainResidueDetails
ATHR157
AGLY222
AGLU243
AASN248
AILE299
AASN346
AHIS353

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.8
ChainResidueDetails
ASER2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER183

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
ChainResidueDetails
ALYS186

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P50247
ChainResidueDetails
ATYR193

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

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PDB entries from 2024-07-17

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