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6ACH

Structure of NAD+-bound leucine dehydrogenase from Geobacillus stearothermophilus by cryo-EM

Functional Information from GO Data
ChainGOidnamespacecontents
A0006520biological_processamino acid metabolic process
A0016491molecular_functionoxidoreductase activity
A0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B0006520biological_processamino acid metabolic process
B0016491molecular_functionoxidoreductase activity
B0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C0006520biological_processamino acid metabolic process
C0016491molecular_functionoxidoreductase activity
C0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
D0006520biological_processamino acid metabolic process
D0016491molecular_functionoxidoreductase activity
D0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
E0006520biological_processamino acid metabolic process
E0016491molecular_functionoxidoreductase activity
E0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
F0006520biological_processamino acid metabolic process
F0016491molecular_functionoxidoreductase activity
F0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
G0006520biological_processamino acid metabolic process
G0016491molecular_functionoxidoreductase activity
G0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
H0006520biological_processamino acid metabolic process
H0016491molecular_functionoxidoreductase activity
H0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue NAD A 400
ChainResidue
ASER147
ALEU239
ASER259
AASN261
ATHR150
AGLY180
AGLY182
AVAL184
AASP203
AILE204
ACYS237
AALA238

site_idAC2
Number of Residues12
Detailsbinding site for residue NAD B 400
ChainResidue
BSER147
BTHR150
BGLY180
BGLY182
BVAL184
BASP203
BILE204
BCYS237
BALA238
BLEU239
BSER259
BASN261

site_idAC3
Number of Residues12
Detailsbinding site for residue NAD C 400
ChainResidue
CSER147
CTHR150
CGLY180
CGLY182
CVAL184
CASP203
CILE204
CCYS237
CALA238
CLEU239
CSER259
CASN261

site_idAC4
Number of Residues12
Detailsbinding site for residue NAD D 400
ChainResidue
DSER147
DTHR150
DGLY180
DGLY182
DVAL184
DASP203
DILE204
DCYS237
DALA238
DLEU239
DSER259
DASN261

site_idAC5
Number of Residues12
Detailsbinding site for residue NAD E 400
ChainResidue
ESER147
ETHR150
EGLY180
EGLY182
EVAL184
EASP203
EILE204
ECYS237
EALA238
ELEU239
ESER259
EASN261

site_idAC6
Number of Residues12
Detailsbinding site for residue NAD F 400
ChainResidue
FSER147
FTHR150
FGLY180
FGLY182
FVAL184
FASP203
FILE204
FCYS237
FALA238
FLEU239
FSER259
FASN261

site_idAC7
Number of Residues12
Detailsbinding site for residue NAD G 400
ChainResidue
GSER147
GTHR150
GGLY180
GGLY182
GVAL184
GASP203
GILE204
GCYS237
GALA238
GLEU239
GSER259
GASN261

site_idAC8
Number of Residues12
Detailsbinding site for residue NAD H 400
ChainResidue
HSER147
HTHR150
HGLY180
HGLY182
HVAL184
HASP203
HILE204
HCYS237
HALA238
HLEU239
HSER259
HASN261

Functional Information from PROSITE/UniProt
site_idPS00074
Number of Residues14
DetailsGLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LnlGGGKtViigDP
ChainResidueDetails
ALEU74-PRO87

224572

PDB entries from 2024-09-04

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