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1JS3

Crystal structure of dopa decarboxylase in complex with the inhibitor carbidopa

Functional Information from GO Data
ChainGOidnamespacecontents
A0004058molecular_functionaromatic-L-amino-acid decarboxylase activity
A0005737cellular_componentcytoplasm
A0006520biological_processamino acid metabolic process
A0006584biological_processcatecholamine metabolic process
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
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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 801
ChainResidue
AASN2
AALA3
BTYR86
BARG453
BLYS454

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
BALA3
ATYR86
AARG453
ALYS454
BASN2

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 803
ChainResidue
AARG347
AHIS348
BHOH941

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 804
ChainResidue
BARG347
BHIS348

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 601
ChainResidue
ASER147
AALA148
ASER149
AHIS192
ASER194
ATHR246
AASP271
AALA273
AASN300
AHIS302
ALYS303
A142701
AHOH805
AHOH908

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP B 602
ChainResidue
BSER147
BALA148
BSER149
BHIS192
BSER194
BTHR246
BASP271
BALA273
BASN300
BHIS302
BLYS303
B142702
BHOH959
BHOH987

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 142 A 701
ChainResidue
ATYR79
APHE80
APRO81
ATHR82
AHIS192
AHIS302
ALYS303
APLP601
AHOH1001
AHOH1003

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 142 B 702
ChainResidue
BTYR79
BPHE80
BPRO81
BTHR82
BHIS192
BTHR246
BHIS302
BLYS303
BPLP602
BHOH1022

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 Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11685243, ECO:0007744|PDB:1JS3
ChainResidueDetails
ATHR82
AHIS192
BTHR82
BHIS192

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P20711
ChainResidueDetails
AALA148
ASER149
ATHR246
AASN300
BALA148
BSER149
BTHR246
BASN300

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:1935935
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11685243
ChainResidueDetails
ALYS303
BLYS303

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PDB entries from 2024-08-07

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