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1K89

K89L MUTANT OF GLUTAMATE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004352molecular_functionglutamate dehydrogenase (NAD+) activity
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
A0019552biological_processglutamate catabolic process via 2-hydroxyglutarate
A0055114biological_processobsolete oxidation-reduction process
Functional Information from PROSITE/UniProt
site_idPS00074
Number of Residues14
DetailsGLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpmGGAKgGsdfDP
ChainResidueDetails
ALEU119-PRO132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10011, ECO:0000269|PubMed:8263917
ChainResidueDetails
AGLY126

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:8263917
ChainResidueDetails
AGLY90
AALA111
AASP114
AASP165
AGLY381

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLY210
AVAL241

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalysis => ECO:0000250
ChainResidueDetails
ALEU166

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 579
ChainResidueDetails
AGLY126electrostatic stabiliser, proton acceptor, proton donor
ALEU166proton acceptor, proton donor

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PDB entries from 2024-11-06

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