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7CGQ

Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase E147A mutant (NADP and L-arabinose bound form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019151molecular_functiongalactose 1-dehydrogenase activity
A0019568biological_processarabinose catabolic process
A0019570biological_processL-arabinose catabolic process to 2-oxoglutarate
A0019572biological_processL-arabinose catabolic process
A0044103molecular_functionL-arabinose 1-dehydrogenase (NADP+) activity
A0047910molecular_functiongalactose 1-dehydrogenase (NADP+) activity
A0050022molecular_functionL-arabinose 1-dehydrogenase (NAD+) activity
A0070401molecular_functionNADP+ binding
A0070403molecular_functionNAD+ binding
B0000166molecular_functionnucleotide binding
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019151molecular_functiongalactose 1-dehydrogenase activity
B0019568biological_processarabinose catabolic process
B0019570biological_processL-arabinose catabolic process to 2-oxoglutarate
B0019572biological_processL-arabinose catabolic process
B0044103molecular_functionL-arabinose 1-dehydrogenase (NADP+) activity
B0047910molecular_functiongalactose 1-dehydrogenase (NADP+) activity
B0050022molecular_functionL-arabinose 1-dehydrogenase (NAD+) activity
B0070401molecular_functionNADP+ binding
B0070403molecular_functionNAD+ binding
C0000166molecular_functionnucleotide binding
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019151molecular_functiongalactose 1-dehydrogenase activity
C0019568biological_processarabinose catabolic process
C0019570biological_processL-arabinose catabolic process to 2-oxoglutarate
C0019572biological_processL-arabinose catabolic process
C0044103molecular_functionL-arabinose 1-dehydrogenase (NADP+) activity
C0047910molecular_functiongalactose 1-dehydrogenase (NADP+) activity
C0050022molecular_functionL-arabinose 1-dehydrogenase (NAD+) activity
C0070401molecular_functionNADP+ binding
C0070403molecular_functionNAD+ binding
D0000166molecular_functionnucleotide binding
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019151molecular_functiongalactose 1-dehydrogenase activity
D0019568biological_processarabinose catabolic process
D0019570biological_processL-arabinose catabolic process to 2-oxoglutarate
D0019572biological_processL-arabinose catabolic process
D0044103molecular_functionL-arabinose 1-dehydrogenase (NADP+) activity
D0047910molecular_functiongalactose 1-dehydrogenase (NADP+) activity
D0050022molecular_functionL-arabinose 1-dehydrogenase (NAD+) activity
D0070401molecular_functionNADP+ binding
D0070403molecular_functionNAD+ binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:B3TMR8
ChainResidueDetails
ALYS91
BLYS91
CLYS91
DLYS91

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:B3TMR8
ChainResidueDetails
AILE15
ASER37
BILE15
BSER37
CILE15
CSER37
DILE15
DSER37

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:B3TMR8, ECO:0000305|PubMed:16326697
ChainResidueDetails
AASP169
BASP169
CASP169
DASP169

221716

PDB entries from 2024-06-26

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