Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2BMA

The crystal structure of Plasmodium falciparum glutamate dehydrogenase, a putative target for novel antimalarial drugs

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
A0004354molecular_functionglutamate dehydrogenase (NADP+) activity
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006537biological_processglutamate biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B0000166molecular_functionnucleotide binding
B0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
B0004354molecular_functionglutamate dehydrogenase (NADP+) activity
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006537biological_processglutamate biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C0000166molecular_functionnucleotide binding
C0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
C0004354molecular_functionglutamate dehydrogenase (NADP+) activity
C0005829cellular_componentcytosol
C0006520biological_processamino acid metabolic process
C0006537biological_processglutamate biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
D0000166molecular_functionnucleotide binding
D0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
D0004354molecular_functionglutamate dehydrogenase (NADP+) activity
D0005829cellular_componentcytosol
D0006520biological_processamino acid metabolic process
D0006537biological_processglutamate biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
E0000166molecular_functionnucleotide binding
E0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
E0004354molecular_functionglutamate dehydrogenase (NADP+) activity
E0005829cellular_componentcytosol
E0006520biological_processamino acid metabolic process
E0006537biological_processglutamate biosynthetic process
E0016491molecular_functionoxidoreductase activity
E0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
F0000166molecular_functionnucleotide binding
F0004353molecular_functionglutamate dehydrogenase [NAD(P)+] activity
F0004354molecular_functionglutamate dehydrogenase (NADP+) activity
F0005829cellular_componentcytosol
F0006520biological_processamino acid metabolic process
F0006537biological_processglutamate biosynthetic process
F0016491molecular_functionoxidoreductase activity
F0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
Functional Information from PROSITE/UniProt
site_idPS00074
Number of Residues14
DetailsGLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LsmGGGKgGsdfDP
ChainResidueDetails
ALEU119-PRO132

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
ALYS125
AASP165

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
BLYS125
BASP165

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
CLYS125
CASP165

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
DLYS125
DASP165

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
ELYS125
EASP165

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hrd
ChainResidueDetails
FLYS125
FASP165

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon