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6JNJ

Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase (apo-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
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue PO4 A 401
ChainResidue
ALYS91
AHIS119
AHIS153
AASP169
AASN173
AHOH535
AHOH573
AHOH621
AHOH670

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 B 401
ChainResidue
BLYS91
BHIS119
BASP169
BASN173
BHOH559
BHOH586

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:B3TMR8
ChainResidueDetails
ALYS91
BLYS91

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:B3TMR8
ChainResidueDetails
AILE15
ASER37
BILE15
BSER37

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:B3TMR8, ECO:0000305|PubMed:16326697
ChainResidueDetails
AASP169
BASP169

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PDB entries from 2024-10-09

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