Structure of PDB 2okj Chain B

Receptor sequence
>2okjB (length=504) Species: 9606 (Homo sapiens) [Search protein sequence]
TDFSNLFARDLLPAKNGEEQTVQFLLEVVDILLNYVRKTFDRSTKVLDFH
HPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGHPRFFNQLS
TGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWSSK
DGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHY
SIKKAGAALGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVN
ATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLNG
IERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQY
DVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYA
KIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAPKI
KALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQ
DLHH
3D structure
PDB2okj GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop.
ChainB
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.15: glutamate decarboxylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ABU B Q190 L191 S192 R567 Q98 L99 S100 R475
BS02 PLZ B L191 G251 G252 A253 H291 T348 D373 A375 N402 H404 X405 L99 G159 G160 A161 H199 T256 D281 A283 N310 H312 X313
Gene Ontology
Molecular Function
GO:0016830 carbon-carbon lyase activity
GO:0016831 carboxy-lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0019752 carboxylic acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2okj, PDBe:2okj, PDBj:2okj
PDBsum2okj
PubMed17384644
UniProtQ99259|DCE1_HUMAN Glutamate decarboxylase 1 (Gene Name=GAD1)

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