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4DAL

Crystal structure of Putative aldehyde dehydrogenase from Sinorhizobium meliloti 1021

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0000166molecular_functionnucleotide binding
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0000166molecular_functionnucleotide binding
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
E0000166molecular_functionnucleotide binding
E0016491molecular_functionoxidoreductase activity
E0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F0000166molecular_functionnucleotide binding
F0016491molecular_functionoxidoreductase activity
F0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
G0000166molecular_functionnucleotide binding
G0016491molecular_functionoxidoreductase activity
G0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
H0000166molecular_functionnucleotide binding
H0016491molecular_functionoxidoreductase activity
H0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 600
ChainResidue
AGLY249
AHOH703
AHOH713
ALYS250
AGLY277
AASP279
ACYS284
AGLU378
AVAL379
APHE380
AGLY381

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 600
ChainResidue
DGLY204
DASN209
DTHR228
DLYS231

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKAP
ChainResidueDetails
ALEU245-PRO252

223790

PDB entries from 2024-08-14

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