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7CGR

Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase E147A mutant (NADP and glycerol 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 PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue NAP A 401
ChainResidue
AGLY13
AVAL72
AARG73
AGLU90
ALYS91
AHIS119
ATRP152
AHIS153
AGLN156
ATRP158
AASP169
ALYS14
ATYR266
AGOL402
AHOH508
AHOH515
AHOH521
AHOH527
AHOH588
AHOH590
AILE15
ASER37
AARG38
AHIS39
ACYS67
AALA68
APRO69

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 402
ChainResidue
ALYS91
AHIS119
ATRP152
AHIS153
AASP169
APRO170
AASN173
ANAP401
AHOH528

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 403
ChainResidue
AGLU27
AALA271
AHIS274
AALA275
AHOH582
DVAL302
DGLN303
DTHR304

site_idAC4
Number of Residues9
Detailsbinding site for residue NAP B 401
ChainResidue
BGLY11
BGLY13
BSER37
BARG38
BHIS39
BALA68
BPRO69
BVAL72
BHOH527

site_idAC5
Number of Residues12
Detailsbinding site for residue NAP C 401
ChainResidue
CGLY11
CGLY13
CSER37
CARG38
CHIS39
CALA68
CPRO69
CVAL72
CTRP158
CHOH573
CHOH595
CHOH619

site_idAC6
Number of Residues28
Detailsbinding site for residue NAP D 401
ChainResidue
DGLY11
DGLY13
DLYS14
DILE15
DSER37
DARG38
DHIS39
DCYS67
DALA68
DPRO69
DPRO70
DVAL72
DARG73
DGLU90
DLYS91
DHIS119
DGLN156
DTRP158
DASP169
DTYR266
DGOL402
DHOH522
DHOH544
DHOH555
DHOH577
DHOH618
DHOH624
DHOH645

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL D 402
ChainResidue
DLYS91
DHIS119
DHIS153
DASN173
DNAP401
DHOH653

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

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PDB entries from 2025-06-18

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