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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 |