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6ENZ

Crystal structure of mouse GADL1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003674molecular_functionmolecular_function
A0004068molecular_functionaspartate 1-decarboxylase activity
A0004782molecular_functionsulfinoalanine decarboxylase activity
A0008150biological_processbiological_process
A0016830molecular_functioncarbon-carbon lyase activity
A0016831molecular_functioncarboxy-lyase activity
A0019752biological_processcarboxylic acid metabolic process
A0030170molecular_functionpyridoxal phosphate binding
B0003674molecular_functionmolecular_function
B0004068molecular_functionaspartate 1-decarboxylase activity
B0004782molecular_functionsulfinoalanine decarboxylase activity
B0008150biological_processbiological_process
B0016830molecular_functioncarbon-carbon lyase activity
B0016831molecular_functioncarboxy-lyase activity
B0019752biological_processcarboxylic acid metabolic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue PLP A 601
ChainResidue
ALEU102
ALYS314
BCYS365
BSER366
AGLY160
AGLY161
ASER162
AHIS200
ATHR257
AASP282
ATRP285
AASN311

site_idAC2
Number of Residues19
Detailsbinding site for Di-peptide PLP B 601 and LYS B 314
ChainResidue
ACYS365
ASER366
BLEU102
BGLY160
BGLY161
BSER162
BHIS200
BGLY255
BTHR257
BASP282
BSER284
BTRP285
BASN311
BPRO312
BHIS313
BMET315
BLEU316
BMET317
BILE479

Functional Information from PROSITE/UniProt
site_idPS00392
Number of Residues22
DetailsDDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SVaWnphKMLmAgIQCsaLLvK
ChainResidueDetails
ASER307-LYS328

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:29372909, ECO:0007744|PDB:6ENZ
ChainResidueDetails
ALYS314
BLYS314

226707

PDB entries from 2024-10-30

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