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1JL0

Structure of a Human S-Adenosylmethionine Decarboxylase Self-processing Ester Intermediate and Mechanism of Putrescine Stimulation of Processing as Revealed by the H243A Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004014molecular_functionadenosylmethionine decarboxylase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006595biological_processpolyamine metabolic process
A0006597biological_processspermine biosynthetic process
A0008295biological_processspermidine biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
A0019810molecular_functionputrescine binding
A0042802molecular_functionidentical protein binding
B0004014molecular_functionadenosylmethionine decarboxylase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006595biological_processpolyamine metabolic process
B0006597biological_processspermine biosynthetic process
B0008295biological_processspermidine biosynthetic process
B0016831molecular_functioncarboxy-lyase activity
B0019810molecular_functionputrescine binding
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PUT A 401
ChainResidue
ALEU13
AHOH3394
AGLU15
APHE111
AASP174
ATHR176
APHE285
ATYR318
AHOH3001
AHOH3018

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 402
ChainResidue
AHIS5
APHE7
ACYS226
APRO246
AGLU247
AHOH3075
AHOH3220
AHOH3361

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PUT B 401
ChainResidue
BLEU13
BGLU15
BPHE111
BASP174
BTHR176
BTYR318
BHOH503
BHOH504
BHOH514

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TRS B 402
ChainResidue
BHIS5
BCYS226
BPRO246
BGLU247
BHOH587
BHOH733

Functional Information from PROSITE/UniProt
site_idPS01336
Number of Residues11
DetailsADOMETDC S-adenosylmethionine decarboxylase signature. AYVLSESSMFV
ChainResidueDetails
AALA62-VAL72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:1917972
ChainResidueDetails
AGLU8
AGLU11
BGLU8
BGLU11

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate; via pyruvic acid => ECO:0000269|PubMed:11583147
ChainResidueDetails
ASER68
BSER68

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor; for catalytic activity => ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:11583147
ChainResidueDetails
ACYS82
BCYS82

site_idSWS_FT_FI4
Number of Residues4
DetailsACT_SITE: Proton acceptor; for processing activity => ECO:0000269|PubMed:11583147
ChainResidueDetails
ASER229
AALA243
BSER229
BALA243

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:11583147
ChainResidueDetails
APHE7
AGLU67
APHE223
AGLU247
BPHE7
BGLU67
BPHE223
BGLU247

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Cleavage (non-hydrolytic); by autolysis => ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270
ChainResidueDetails
AGLU67
BGLU67

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Pyruvic acid (Ser); by autocatalysis => ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270
ChainResidueDetails
ASER68
BSER68

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER298
BSER298

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1jen
ChainResidueDetails
AALA243
ASER229
ACYS82
BGLU11
BGLU67

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1jen
ChainResidueDetails
AGLU11
AGLU67
BSER229
BALA243
BCYS82

site_idMCSA1
Number of Residues5
DetailsM-CSA 575
ChainResidueDetails
AGLU67
ASER68covalently attached, electron shuttle
ACYS82proton shuttle (general acid/base)
ASER229
AALA243

site_idMCSA2
Number of Residues5
DetailsM-CSA 575
ChainResidueDetails
BGLU67
BSER68covalently attached, electron shuttle
BCYS82proton shuttle (general acid/base)
BSER229
BALA243

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PDB entries from 2024-05-01

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