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2OKJ

The X-ray crystal structure of the 67kDa isoform of Glutamic Acid Decarboxylase (GAD67)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016830molecular_functioncarbon-carbon lyase activity
A0016831molecular_functioncarboxy-lyase activity
A0019752biological_processcarboxylic acid metabolic process
A0030170molecular_functionpyridoxal phosphate binding
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 Residues5
DetailsBINDING SITE FOR RESIDUE ABU A 1001
ChainResidue
AGLN190
ALEU191
ASER192
AARG567
BTYR434

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ABU B 1002
ChainResidue
BSER192
BARG567
BPLZ2001
ALEU435
BASN189
BGLN190
BLEU191

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE PLZ B 2001
ChainResidue
APHE214
ACYS455
AGLY456
BGLN190
BLEU191
BSER192
BGLY251
BGLY252
BALA253
BHIS291
BGLY346
BTHR348
BASP373
BALA375
BASN402
BHIS404
BLLP405
BABU1002
BHOH2030
BHOH2035

Functional Information from PROSITE/UniProt
site_idPS00392
Number of Residues22
DetailsDDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SVtWnphKMMgVlLQCsaILvK
ChainResidueDetails
ASER398-LYS419

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17384644, ECO:0007744|PDB:2OKJ
ChainResidueDetails
BGLN190
BARG567
AGLN190
AARG567

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:17384644, ECO:0007744|PDB:2OKJ
ChainResidueDetails
ALLP405
BLLP405

218500

PDB entries from 2024-04-17

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