3IJR
2.05 Angstrom resolution crystal structure of a short chain dehydrogenase from Bacillus anthracis str. 'Ames Ancestor' in complex with NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008206 | biological_process | bile acid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008206 | biological_process | bile acid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008206 | biological_process | bile acid metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008206 | biological_process | bile acid metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0008206 | biological_process | bile acid metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0008206 | biological_process | bile acid metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0008206 | biological_process | bile acid metabolic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0008206 | biological_process | bile acid metabolic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD A 301 |
| Chain | Residue |
| A | ASP53 |
| A | LEU103 |
| A | ASN129 |
| A | VAL130 |
| A | ALA131 |
| A | GLN132 |
| A | ILE153 |
| A | TYR158 |
| A | THR178 |
| A | ALA179 |
| A | SER180 |
| A | SER54 |
| A | TYR193 |
| A | LYS197 |
| A | PRO223 |
| A | GLY224 |
| A | PRO225 |
| A | ILE226 |
| A | THR228 |
| A | PRO229 |
| A | LEU230 |
| A | ILE231 |
| A | GLY55 |
| A | PHE243 |
| A | HOH291 |
| A | MG300 |
| A | HOH318 |
| A | HOH428 |
| A | HOH816 |
| A | ILE56 |
| A | TYR75 |
| A | LEU76 |
| A | GLU78 |
| A | GLY101 |
| A | ASP102 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 300 |
| Chain | Residue |
| A | ASP53 |
| A | SER54 |
| A | GLU78 |
| A | NAD301 |
| A | HOH428 |
| A | HOH918 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 317 |
| Chain | Residue |
| A | LYS110 |
| A | LYS163 |
| A | HOH679 |
| A | HOH801 |
| A | HOH804 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 323 |
| Chain | Residue |
| A | SER122 |
| A | ASN124 |
| A | LYS170 |
| A | HOH321 |
| A | HOH396 |
| A | HOH808 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD B 301 |
| Chain | Residue |
| B | PRO19 |
| B | GLY51 |
| B | ASP53 |
| B | SER54 |
| B | GLY55 |
| B | ILE56 |
| B | TYR75 |
| B | LEU76 |
| B | GLU78 |
| B | GLY101 |
| B | ASP102 |
| B | LEU103 |
| B | ASN129 |
| B | VAL130 |
| B | ALA131 |
| B | GLN132 |
| B | ILE153 |
| B | THR178 |
| B | ALA179 |
| B | SER180 |
| B | TYR193 |
| B | LYS197 |
| B | PRO223 |
| B | GLY224 |
| B | PRO225 |
| B | ILE226 |
| B | THR228 |
| B | PRO229 |
| B | LEU230 |
| B | ILE231 |
| B | PHE243 |
| B | MG300 |
| B | HOH319 |
| B | HOH795 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 300 |
| Chain | Residue |
| B | ASP53 |
| B | SER54 |
| B | GLU78 |
| B | NAD301 |
| B | HOH795 |
| B | HOH796 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 318 |
| Chain | Residue |
| B | LYS110 |
| B | LYS163 |
| B | HOH841 |
| B | HOH851 |
| B | HOH858 |
| B | HOH922 |
| C | HOH936 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD C 301 |
| Chain | Residue |
| C | ASP53 |
| C | SER54 |
| C | GLY55 |
| C | ILE56 |
| C | TYR75 |
| C | LEU76 |
| C | GLU78 |
| C | GLY101 |
| C | ASP102 |
| C | LEU103 |
| C | ASN129 |
| C | VAL130 |
| C | ALA131 |
| C | GLN132 |
| C | ILE153 |
| C | TYR158 |
| C | THR178 |
| C | ALA179 |
| C | SER180 |
| C | TYR193 |
| C | LYS197 |
| C | PRO223 |
| C | GLY224 |
| C | PRO225 |
| C | ILE226 |
| C | THR228 |
| C | PRO229 |
| C | LEU230 |
| C | ILE231 |
| C | PHE243 |
| C | MG300 |
| C | HOH302 |
| C | HOH380 |
| C | HOH473 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 300 |
| Chain | Residue |
| C | ASP53 |
| C | SER54 |
| C | GLU78 |
| C | NAD301 |
| C | HOH380 |
| C | HOH697 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 320 |
| Chain | Residue |
| C | GLU106 |
| C | LYS110 |
| C | LYS163 |
| C | HOH313 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 321 |
| Chain | Residue |
| C | SER122 |
| C | ASN124 |
| C | HOH342 |
| C | HOH365 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 327 |
| Chain | Residue |
| C | LYS170 |
| C | GLN171 |
| C | HOH940 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 328 |
| Chain | Residue |
| C | GLY172 |
| C | ARG217 |
| C | SER267 |
| C | SER268 |
| C | SER271 |
| C | HOH350 |
| C | HOH900 |
| C | HOH913 |
| site_id | BC5 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD D 301 |
| Chain | Residue |
| D | PRO19 |
| D | ASP53 |
| D | SER54 |
| D | GLY55 |
| D | ILE56 |
| D | TYR75 |
| D | LEU76 |
| D | GLU78 |
| D | GLY101 |
| D | ASP102 |
| D | LEU103 |
| D | ASN129 |
| D | VAL130 |
| D | ALA131 |
| D | GLN132 |
| D | ILE153 |
| D | THR178 |
| D | ALA179 |
| D | SER180 |
| D | TYR193 |
| D | LYS197 |
| D | PRO223 |
| D | GLY224 |
| D | PRO225 |
| D | ILE226 |
| D | THR228 |
| D | PRO229 |
| D | LEU230 |
| D | ILE231 |
| D | PHE243 |
| D | MG300 |
| D | HOH307 |
| D | HOH476 |
| D | HOH487 |
| D | HOH849 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 300 |
| Chain | Residue |
| D | ASP53 |
| D | SER54 |
| D | GLU78 |
| D | NAD301 |
| D | HOH738 |
| D | HOH849 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 324 |
| Chain | Residue |
| A | THR143 |
| A | HOH845 |
| D | LYS110 |
| D | LYS163 |
| site_id | BC8 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD E 301 |
| Chain | Residue |
| E | ASP53 |
| E | SER54 |
| E | GLY55 |
| E | ILE56 |
| E | TYR75 |
| E | LEU76 |
| E | GLU78 |
| E | GLY101 |
| E | ASP102 |
| E | LEU103 |
| E | ASN129 |
| E | VAL130 |
| E | ALA131 |
| E | GLN132 |
| E | ILE153 |
| E | TYR158 |
| E | THR178 |
| E | ALA179 |
| E | SER180 |
| E | TYR193 |
| E | LYS197 |
| E | PRO223 |
| E | GLY224 |
| E | ILE226 |
| E | THR228 |
| E | PRO229 |
| E | LEU230 |
| E | ILE231 |
| E | PHE243 |
| E | MG300 |
| E | HOH502 |
| E | HOH552 |
| E | HOH645 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 300 |
| Chain | Residue |
| E | ASP53 |
| E | SER54 |
| E | GLU78 |
| E | NAD301 |
| E | HOH645 |
| E | HOH815 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 E 319 |
| Chain | Residue |
| E | GLU106 |
| E | LYS110 |
| E | LYS163 |
| E | HOH784 |
| H | THR143 |
| site_id | CC2 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD F 301 |
| Chain | Residue |
| F | PRO19 |
| F | ASP53 |
| F | SER54 |
| F | GLY55 |
| F | ILE56 |
| F | TYR75 |
| F | LEU76 |
| F | GLU78 |
| F | GLY101 |
| F | ASP102 |
| F | LEU103 |
| F | ASN129 |
| F | VAL130 |
| F | ALA131 |
| F | GLN132 |
| F | ILE153 |
| F | TYR158 |
| F | THR178 |
| F | ALA179 |
| F | SER180 |
| F | TYR193 |
| F | LYS197 |
| F | PRO223 |
| F | GLY224 |
| F | PRO225 |
| F | ILE226 |
| F | THR228 |
| F | PRO229 |
| F | LEU230 |
| F | ILE231 |
| F | PHE243 |
| F | MG300 |
| F | HOH305 |
| F | HOH752 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 300 |
| Chain | Residue |
| F | ASP53 |
| F | SER54 |
| F | GLU78 |
| F | NAD301 |
| F | HOH751 |
| F | HOH752 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 F 322 |
| Chain | Residue |
| F | SER122 |
| F | ASN124 |
| F | LYS170 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 F 326 |
| Chain | Residue |
| F | LYS110 |
| F | LYS163 |
| F | HOH560 |
| F | HOH701 |
| G | THR143 |
| site_id | CC6 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD G 301 |
| Chain | Residue |
| G | PRO19 |
| G | ASP53 |
| G | SER54 |
| G | GLY55 |
| G | ILE56 |
| G | TYR75 |
| G | LEU76 |
| G | GLU78 |
| G | GLY101 |
| G | ASP102 |
| G | LEU103 |
| G | ASN129 |
| G | VAL130 |
| G | ALA131 |
| G | GLN132 |
| G | ILE153 |
| G | TYR158 |
| G | THR178 |
| G | ALA179 |
| G | SER180 |
| G | TYR193 |
| G | LYS197 |
| G | PRO223 |
| G | GLY224 |
| G | PRO225 |
| G | ILE226 |
| G | THR228 |
| G | PRO229 |
| G | LEU230 |
| G | ILE231 |
| G | PHE243 |
| G | MG300 |
| G | HOH384 |
| G | HOH522 |
| G | HOH600 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG G 300 |
| Chain | Residue |
| G | ASP53 |
| G | SER54 |
| G | GLU78 |
| G | NAD301 |
| G | HOH480 |
| G | HOH522 |
| site_id | CC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 G 329 |
| Chain | Residue |
| F | THR143 |
| G | LYS110 |
| G | LYS163 |
| G | HOH814 |
| site_id | CC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 G 330 |
| Chain | Residue |
| G | GLY172 |
| G | VAL174 |
| G | ARG217 |
| G | SER267 |
| G | SER268 |
| G | SER271 |
| G | HOH617 |
| G | HOH937 |
| site_id | DC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAD H 301 |
| Chain | Residue |
| H | ASP53 |
| H | SER54 |
| H | GLY55 |
| H | ILE56 |
| H | TYR75 |
| H | LEU76 |
| H | GLU78 |
| H | GLY101 |
| H | ASP102 |
| H | LEU103 |
| H | ASN129 |
| H | VAL130 |
| H | ALA131 |
| H | GLN132 |
| H | ILE153 |
| H | TYR158 |
| H | THR178 |
| H | ALA179 |
| H | SER180 |
| H | TYR193 |
| H | LYS197 |
| H | PRO223 |
| H | GLY224 |
| H | PRO225 |
| H | ILE226 |
| H | THR228 |
| H | PRO229 |
| H | LEU230 |
| H | ILE231 |
| H | PHE243 |
| H | MG300 |
| H | HOH479 |
| H | HOH492 |
| H | HOH527 |
| H | HOH605 |
| H | HOH634 |
| site_id | DC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 300 |
| Chain | Residue |
| H | ASP53 |
| H | SER54 |
| H | GLU78 |
| H | NAD301 |
| H | HOH474 |
| H | HOH527 |
| site_id | DC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 H 325 |
| Chain | Residue |
| H | GLU106 |
| H | LYS110 |
| H | LYS163 |
| H | HOH416 |
| H | HOH776 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SivayegnetLidYSATKGAIvAFTrSLS |
| Chain | Residue | Details |
| A | SER180-SER208 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER180 | |
| A | TYR193 | |
| A | LYS197 |
| site_id | CSA10 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR193 | |
| B | SER180 | |
| B | ASN154 | |
| B | LYS197 |
| site_id | CSA11 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR193 | |
| C | SER180 | |
| C | ASN154 | |
| C | LYS197 |
| site_id | CSA12 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR193 | |
| D | SER180 | |
| D | ASN154 | |
| D | LYS197 |
| site_id | CSA13 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | TYR193 | |
| E | SER180 | |
| E | ASN154 | |
| E | LYS197 |
| site_id | CSA14 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | TYR193 | |
| F | SER180 | |
| F | ASN154 | |
| F | LYS197 |
| site_id | CSA15 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | TYR193 | |
| G | SER180 | |
| G | ASN154 | |
| G | LYS197 |
| site_id | CSA16 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | TYR193 | |
| H | SER180 | |
| H | ASN154 | |
| H | LYS197 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS197 | |
| A | LEU190 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS197 | |
| B | LEU190 |
| site_id | CSA19 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS197 | |
| C | LEU190 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER180 | |
| B | TYR193 | |
| B | LYS197 |
| site_id | CSA20 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS197 | |
| D | LEU190 |
| site_id | CSA21 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | LYS197 | |
| E | LEU190 |
| site_id | CSA22 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | LYS197 | |
| F | LEU190 |
| site_id | CSA23 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | LYS197 | |
| G | LEU190 |
| site_id | CSA24 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | LYS197 | |
| H | LEU190 |
| site_id | CSA25 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR193 | |
| A | LYS197 |
| site_id | CSA26 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR193 | |
| B | LYS197 |
| site_id | CSA27 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR193 | |
| C | LYS197 |
| site_id | CSA28 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | TYR193 | |
| D | LYS197 |
| site_id | CSA29 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | TYR193 | |
| E | LYS197 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER180 | |
| C | TYR193 | |
| C | LYS197 |
| site_id | CSA30 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | TYR193 | |
| F | LYS197 |
| site_id | CSA31 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | TYR193 | |
| G | LYS197 |
| site_id | CSA32 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | TYR193 | |
| H | LYS197 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | SER180 | |
| D | TYR193 | |
| D | LYS197 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | SER180 | |
| E | TYR193 | |
| E | LYS197 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| F | SER180 | |
| F | TYR193 | |
| F | LYS197 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| G | SER180 | |
| G | TYR193 | |
| G | LYS197 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| H | SER180 | |
| H | TYR193 | |
| H | LYS197 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR193 | |
| A | SER180 | |
| A | ASN154 | |
| A | LYS197 |
