5ITW
Crystal structure of Bacillus subtilis BacC Dihydroanticapsin 7-dehydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0017000 | biological_process | antibiotic biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0017000 | biological_process | antibiotic biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue SO4 A 301 |
Chain | Residue |
A | MET1 |
A | ILE2 |
A | HOH414 |
A | HOH471 |
A | HOH504 |
A | HOH535 |
B | MET1 |
B | GLN30 |
B | HOH458 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | SER17 |
A | GLY18 |
A | ILE19 |
A | GLY20 |
A | ASN89 |
A | HOH404 |
A | HOH408 |
A | HOH416 |
A | HOH427 |
A | HOH473 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
A | MET1 |
A | GLN30 |
B | MET1 |
B | ILE2 |
B | HOH458 |
B | HOH471 |
B | HOH493 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue SO4 C 301 |
Chain | Residue |
C | SER17 |
C | GLY18 |
C | ILE19 |
C | GLY20 |
C | ASN89 |
C | HOH416 |
C | HOH421 |
C | HOH424 |
C | HOH431 |
C | HOH436 |
C | HOH516 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 302 |
Chain | Residue |
C | MET1 |
C | GLN30 |
D | MET1 |
D | ILE2 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 303 |
Chain | Residue |
C | MET1 |
C | ILE2 |
D | MET1 |
D | GLN30 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue SO4 D 301 |
Chain | Residue |
D | SER17 |
D | GLY18 |
D | ILE19 |
D | GLY20 |
D | ASN89 |
D | HOH401 |
D | HOH404 |
D | HOH407 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue SO4 D 302 |
Chain | Residue |
B | ASN107 |
B | LEU110 |
B | THR115 |
B | HOH410 |
D | ASN107 |
D | LEU110 |
D | THR115 |
D | HOH403 |
D | HOH411 |
D | HOH446 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvgglvawpdIpaYNASKGGVlQLTkSMA |
Chain | Residue | Details |
A | SER141-ALA169 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
Chain | Residue | Details |
A | TYR154 | |
B | TYR154 | |
C | TYR154 | |
D | TYR154 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P16544 |
Chain | Residue | Details |
A | LEU11 | |
A | SER141 | |
B | LEU11 | |
B | SER141 | |
C | LEU11 | |
C | SER141 | |
D | LEU11 | |
D | SER141 |