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1JS6

Crystal Structure of DOPA decarboxylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004058molecular_functionaromatic-L-amino-acid decarboxylase activity
A0005737cellular_componentcytoplasm
A0006520biological_processamino acid metabolic process
A0006584biological_processcatecholamine metabolic process
A0016829molecular_functionlyase activity
A0016830molecular_functioncarbon-carbon lyase activity
A0016831molecular_functioncarboxy-lyase activity
A0019752biological_processcarboxylic acid metabolic process
A0030170molecular_functionpyridoxal phosphate binding
A0036467molecular_function5-hydroxy-L-tryptophan decarboxylase activity
A0036468molecular_functionL-dopa decarboxylase activity
A0042416biological_processdopamine biosynthetic process
A0042423biological_processcatecholamine biosynthetic process
A0042427biological_processserotonin biosynthetic process
B0004058molecular_functionaromatic-L-amino-acid decarboxylase activity
B0005737cellular_componentcytoplasm
B0006520biological_processamino acid metabolic process
B0006584biological_processcatecholamine metabolic process
B0016829molecular_functionlyase activity
B0016830molecular_functioncarbon-carbon lyase activity
B0016831molecular_functioncarboxy-lyase activity
B0019752biological_processcarboxylic acid metabolic process
B0030170molecular_functionpyridoxal phosphate binding
B0036467molecular_function5-hydroxy-L-tryptophan decarboxylase activity
B0036468molecular_functionL-dopa decarboxylase activity
B0042416biological_processdopamine biosynthetic process
B0042423biological_processcatecholamine biosynthetic process
B0042427biological_processserotonin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP A 601
ChainResidue
APHE80
AHIS302
ALYS303
AHOH609
BHOH604
ASER147
AALA148
ASER149
AHIS192
ATHR246
AASP271
AALA273
AASN300

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP B 602
ChainResidue
BPHE80
BSER147
BALA148
BSER149
BHIS192
BTHR246
BASP271
BALA273
BASN300
BHIS302
BLYS303
BHOH620
BHOH624

Functional Information from PROSITE/UniProt
site_idPS00392
Number of Residues22
DetailsDDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SFnFnphKWLlVnFDCsaMWvK
ChainResidueDetails
ASER296-LYS317

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues114
DetailsRepeat: {"description":"1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues120
DetailsRepeat: {"description":"2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues240
DetailsRegion: {"description":"2 X approximate tandem repeats"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11685243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JS3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P20711","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"1935935","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"11685243","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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