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

7KQV

Crystal Structure of aldehyde dehydrogenase (ChALDH) from Cladosporium herbarum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
B0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
C0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
C0005737cellular_componentcytoplasm
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
D0004029molecular_functionaldehyde dehydrogenase (NAD+) activity
D0005737cellular_componentcytoplasm
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0043878molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity
Functional Information from PROSITE/UniProt
site_idPS00070
Number of Residues12
DetailsALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNHGQCCCAGS
ChainResidueDetails
APHE290-SER301

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP
ChainResidueDetails
ALEU262-PRO269

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AGLU263
ACYS296
BGLU263
BCYS296
CGLU263
CCYS296
DGLU263
DCYS296

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon