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5ITV

Crystal structure of Bacillus subtilis BacC Dihydroanticapsin 7-dehydrogenase in complex with NADH

Functional Information from GO Data
ChainGOidnamespacecontents
A0008206biological_processbile acid metabolic process
A0016491molecular_functionoxidoreductase activity
A0017000biological_processantibiotic biosynthetic process
B0008206biological_processbile acid metabolic process
B0016491molecular_functionoxidoreductase activity
B0017000biological_processantibiotic biosynthetic process
C0008206biological_processbile acid metabolic process
C0016491molecular_functionoxidoreductase activity
C0017000biological_processantibiotic biosynthetic process
D0008206biological_processbile acid metabolic process
D0016491molecular_functionoxidoreductase activity
D0017000biological_processantibiotic biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue NAI A 301
ChainResidue
AGLY14
AASN89
AALA90
AGLY91
ATHR139
ACYS140
ASER141
ATYR154
ALYS158
APRO184
AGLY185
ASER17
AILE186
AILE187
ATHR189
ALEU191
AASN192
AHOH410
AGLY18
AILE19
AASP38
AILE39
ATHR61
AASP62
AILE63

site_idAC2
Number of Residues24
Detailsbinding site for residue NAI B 301
ChainResidue
BGLY14
BSER17
BGLY18
BILE19
BASP38
BILE39
BTHR61
BASP62
BILE63
BASN89
BGLY91
BTHR139
BCYS140
BSER141
BTYR154
BLYS158
BPRO184
BGLY185
BILE186
BILE187
BTHR189
BLEU191
BASN192
BHOH426

site_idAC3
Number of Residues25
Detailsbinding site for residue NAI C 301
ChainResidue
CGLY14
CSER17
CGLY18
CILE19
CASP38
CILE39
CTHR61
CASP62
CILE63
CASN89
CALA90
CGLY91
CTHR139
CCYS140
CSER141
CTYR154
CLYS158
CPRO184
CGLY185
CILE186
CILE187
CTHR189
CLEU191
CASN192
CHOH401

site_idAC4
Number of Residues19
Detailsbinding site for residue NAI D 301
ChainResidue
DGLY14
DSER17
DGLY18
DILE19
DASP38
DILE39
DTHR61
DASP62
DILE63
DASN89
DTHR139
DCYS140
DSER141
DTYR154
DLYS158
DPRO184
DGLY185
DILE187
DHOH409

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvgglvawpdIpaYNASKGGVlQLTkSMA
ChainResidueDetails
ASER141-ALA169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR154
BTYR154
CTYR154
DTYR154

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P16544
ChainResidueDetails
ALEU11
ASER141
BLEU11
BSER141
CLEU11
CSER141
DLEU11
DSER141

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PDB entries from 2025-06-25

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