_EC 4.1.1.15 Glutamate decarboxylase. 18 PDB entries  
EC 4.-.-.- Lyases. [3,670 PDB entries]
EC 4.1.-.- Carbon-carbon lyases. [1,229 PDB entries]
EC 4.1.1.- Carboxy-lyases. [727 PDB entries]
EC 4.1.1.15 Glutamate decarboxylase. [18 PDB entries]    
1es0

Reaction: L-glutamate = 4-aminobutanoate + CO(2).
 


L-glutamate
=
4-aminobutanoate
+
CO(2)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): L-glutamate 1-carboxy-lyase.
Cofactor(s): Pyridoxal 5'-phosphate.
 

Pyridoxal 5'-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 18 PDB entries in enzyme class E.C.4.1.1.15

  PDB code Protein
1es0
Crystal structure of the murine class ii allele i-a(g7) comp the glutamic acid decarboxylase (gad65) peptide 207-220
Source: Mus musculus. Mouse. Organism_taxid: 10090. Homo sapiens. Human. Organism_taxid: 9606.
Chain: B (190 residues) CATH domains: 3.10.320.10 2.60.40.10
1nwd
Solution structure of ca2+/calmodulin bound to thE C- terminal domain of petunia glutamate decarboxylase
Source: Xenopus laevis. African clawed frog. Organism_taxid: 8355. Gene: (calm1 or cam1 or calm or cam) and (calm2 or cam2 or camb) and (calm3 or cam3 or camc). Expressed in: escherichia coli. Expression_system_taxid: 562. Petunia x hybrida. Organism_taxid: 4102.
Chains: B, C (28 residues)
1pmm
Crystal structure of escherichia coli gadb (low ph)
Source: Escherichia coli. Organism_taxid: 562. Gene: gadb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (450 residues) CATH domains: Unassigned 3.40.640.10
Bound ligands:   Het Group ACY is 75.00% similar to enzyme product CO(2)
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
1pmo
Crystal structure of escherichia coli gadb (neutral ph)
Source: Escherichia coli. Organism_taxid: 562. Gene: gadb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (455 residues) CATH domains: Unassigned 3.40.640.10
Bound ligand:   Het Group PLR is 93.00% similar to enzyme cofactor pyridoxal 5'-phosphate
1xey
Crystal structure of the complex of escherichia coli gada wi glutarate at 2.05 a resolution
Source: Escherichia coli. Organism_taxid: 562. Gene: gada. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Chains: A, B (448 residues) CATH domains: Unassigned 3.40.640.10
Bound ligands:   Het Group GUA is 90.00% similar to enzyme reactant L-glutamate
  Het Group ACT is 75.00% similar to enzyme product CO(2)
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2dgk
Crystal structure of an n-terminal deletion mutant of escher gadb in an autoinhibited state (aldamine)
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: gadb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (438 residues) CATH domain: 3.40.640.10
Bound ligands:   Het Group EDO is 40.00% similar to enzyme product CO(2)
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2dgl
Crystal structure of escherichia coli gadb in complex with b
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: gadb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (450 residues) CATH domains: Unassigned 3.40.640.10
Bound ligands:   Het Group ACY is 75.00% similar to enzyme product CO(2)
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2dgm
Crystal structure of escherichia coli gadb in complex with i
Source: Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: gadb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (452 residues) CATH domains: Unassigned 3.40.640.10
Bound ligands:   Het Group ACY is 57.14% similar to enzyme product 4-aminobutanoate
  Het Group FMT corresponds to enzyme product CO(2)
  Het Group PLP is 93.75% similar to enzyme cofactor pyridoxal
2ojw
Crystal structure of human glutamine synthetase in complex w and phosphate
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: glul, glns. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D, E (360 residues) CATH domains: Unassigned Unassigned
Bound ligands:   Het Group GOL is 44.44% similar to enzyme product 4-aminobutanoate
  Het Group ADP is 43.33% similar to enzyme cofactor pyridoxal
2okj
The x-ray crystal structure of the 67kda isoform of glutamic acid decarboxylase (gad67)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gad1, gad, gad67. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Chains: A, B (501 residues) CATH domains: Unassigned 3.40.640.10
Bound ligands:   Het Group ABU corresponds to enzyme product 4-aminobutanoate
  Het Group PLZ is 65.00% similar to enzyme cofactor pyridoxal 5'-phosphate
2okk
The x-ray crystal structure of the 65kda isoform of glutamic decarboxylase (gad65)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gad2, gad65. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Chain: A (483 residues) CATH domains: Unassigned 3.40.640.10
Bound ligand:   Het Group ABU corresponds to enzyme product 4-aminobutanoate
2qc8
Crystal structure of human glutamine synthetase in complex w and methionine sulfoximine phosphate
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: glul, glns. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H, I, J (356 residues) CATH domains: Unassigned Unassigned
Bound ligand:   Het Group ADP is 43.33% similar to enzyme cofactor pyridoxal
2uu7
Crystal structure of apo glutamine synthetase from dog ( canis familiaris)
Source: Canis familiaris. Dog. Organism_taxid: 9615. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O (370 residues) CATH domains: Unassigned Unassigned
3fz6
Crystal structure of glutamate decarboxylase beta from esche coli: complex with xenon
Source: Escherichia coli k-12. Organism_taxid: 83333. Gene: b1493, gadb, jw1488. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (455 residues) CATH domains: Unassigned 3.40.640.10
Bound ligand:   Het Group PMP is 88.24% similar to enzyme cofactor pyridoxal
3fz7
Crystal structure of apo glutamate decarboxylase beta from e coli
Source: Escherichia coli k-12. Organism_taxid: 83333. Gene: b1493, gadb, jw1488. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (454 residues) CATH domains: Unassigned 3.40.640.10
3fz8
Crystal structure of glutamate decarboxylase beta from esche coli: reduced schiff base with plp
Source: Escherichia coli k-12. Organism_taxid: 83333. Gene: b1493, gadb, jw1488. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (455 residues) CATH domains: Unassigned 3.40.640.10
Bound ligand:   Het Group PLR is 93.75% similar to enzyme cofactor pyridoxal
3hbx
Crystal structure of gad1 from arabidopsis thaliana
Source: Arabidopsis thaliana. Mouse-ear cress,thale-cress. Organism_taxid: 3702. Gene: at5g17330, gad, gad1, gdh1, mkp11.30, mkp11_18. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (437 residues) CATH domains: Unassigned 3.40.640.10
3vp6
Structural characterization of glutamic acid decarboxylase; into the mechanism of autoinactivation
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: gad1. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Chains: A, B (500 residues) CATH domains: Unassigned 3.40.640.10
Bound ligand:   Het Group HLD is 43.75% similar to enzyme reactant L-glutamate