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3RBF

Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the apo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0001822biological_processkidney development
A0004058molecular_functionaromatic-L-amino-acid decarboxylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006584biological_processcatecholamine metabolic process
A0009636biological_processresponse to toxic substance
A0010467biological_processgene expression
A0016829molecular_functionlyase activity
A0016830molecular_functioncarbon-carbon lyase activity
A0016831molecular_functioncarboxy-lyase activity
A0019752biological_processcarboxylic acid metabolic process
A0019899molecular_functionenzyme binding
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
A0070062cellular_componentextracellular exosome
B0001822biological_processkidney development
B0004058molecular_functionaromatic-L-amino-acid decarboxylase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006584biological_processcatecholamine metabolic process
B0009636biological_processresponse to toxic substance
B0010467biological_processgene expression
B0016829molecular_functionlyase activity
B0016830molecular_functioncarbon-carbon lyase activity
B0016831molecular_functioncarboxy-lyase activity
B0019752biological_processcarboxylic acid metabolic process
B0019899molecular_functionenzyme binding
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
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLP A 481
ChainResidue
ASER147
ALYS303
AALA148
ASER149
AHIS192
ATHR246
AASP271
AALA273
AASN300
AHIS302

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 481
ChainResidue
BLYS303
BTRP304

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 482
ChainResidue
BPRO282
BARG285

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:0000250|UniProtKB:P80041
ChainResidueDetails
ATHR82
AHIS192
BTHR82
BHIS192

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22143761, ECO:0007744|PDB:3RCH
ChainResidueDetails
AALA148
ASER149
ATHR246
AASN300
BALA148
BSER149
BTHR246
BASN300

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P80041
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:22143761
ChainResidueDetails
ALYS303
BLYS303

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PDB entries from 2024-04-24

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