Horse liver F93W alcohol dehydrogenase complexed with NAD and pentafluorobenzyl alcohol. Determined by X-ray diffraction at 1.1 Å resolution. Released 22 May 2019.
Explore 6OWM in 3D Show helices and sheets RCSB PDB PDBe
6OWM contains 45 α-helices and 46 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6 | 1 | |
| β-strand | 7-14 | 8 | 1 |
| β-strand | 22-28 | 7 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 35-44 | 10 | 2 |
| α-helix | 47-54 | 8 | |
| β-strand | 63-64 | 2 | 1 |
| β-strand | 68-76 | 9 | 2 |
| β-strand | 88-91 | 4 | 2 |
| α-helix | 101-104 | 4 | |
| β-strand | 130-132 | 3 | 1 |
| β-strand | 135-138 | 4 | 1 |
| β-strand | 147 | 1 | 1 |
| β-strand | 149-153 | 5 | 2 |
| α-helix | 154-156 | 3 | |
| β-strand | 157-159 | 3 | 2 |
| α-helix | 166-169 | 4 | |
| α-helix | 170-173 | 4 | |
| α-helix | 175-181 | 7 | |
| α-helix | 182-187 | 6 | |
| β-strand | 194-198 | 5 | 3 |
| α-helix | 202-213 | 12 | |
| β-strand | 218-222 | 5 | 3 |
| α-helix | 226-228 | 3 | |
| α-helix | 229-235 | 7 | |
| β-strand | 239-241 | 3 | 3 |
| α-helix | 243-245 | 3 | |
| α-helix | 250-257 | 8 | |
| β-strand | 262 | 1 | 4 |
| β-strand | 264-267 | 4 | 3 |
| α-helix | 272-281 | 10 | |
| β-strand | 282 | 1 | 4 |
| β-strand | 288-291 | 4 | 3 |
| α-helix | 299-300 | 2 | |
| β-strand | 301-303 | 3 | 5 |
| α-helix | 306-309 | 4 | |
| β-strand | 313-316 | 4 | 3 |
| α-helix | 319-321 | 3 | |
| α-helix | 324-336 | 13 | |
| α-helix | 343-345 | 3 | |
| β-strand | 346-351 | 6 | 2 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-363 | 9 | |
| β-strand | 369-373 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6 | 1 | |
| β-strand | 7-13 | 7 | 6 |
| β-strand | 14 | 1 | 7 |
| α-helix | 20-21 | 2 | |
| β-strand | 22-28 | 7 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 35-44 | 10 | 8 |
| α-helix | 47-54 | 8 | |
| β-strand | 63 | 1 | 7 |
| β-strand | 69-76 | 8 | 8 |
| β-strand | 88-91 | 4 | 8 |
| α-helix | 101-104 | 4 | |
| β-strand | 130-132 | 3 | 6 |
| β-strand | 135-137 | 3 | 6 |
| β-strand | 138 | 1 | 7 |
| β-strand | 147 | 1 | 6 |
| β-strand | 149-153 | 5 | 8 |
| α-helix | 154-156 | 3 | |
| β-strand | 157-159 | 3 | 8 |
| α-helix | 166-169 | 4 | |
| α-helix | 170-173 | 4 | |
| α-helix | 175-181 | 7 | |
| α-helix | 182-187 | 6 | |
| α-helix | 189-190 | 2 | |
| β-strand | 194-198 | 5 | 3 |
| α-helix | 202-213 | 12 | |
| β-strand | 218-222 | 5 | 3 |
| α-helix | 226-228 | 3 | |
| α-helix | 229-235 | 7 | |
| β-strand | 239-241 | 3 | 3 |
| α-helix | 243-245 | 3 | |
| α-helix | 250-257 | 8 | |
| β-strand | 262 | 1 | 9 |
| β-strand | 264-267 | 4 | 3 |
| α-helix | 272-281 | 10 | |
| β-strand | 282 | 1 | 9 |
| β-strand | 288-291 | 4 | 3 |
| β-strand | 301-303 | 3 | 5 |
| α-helix | 306-309 | 4 | |
| β-strand | 313-316 | 4 | 3 |
| α-helix | 319-321 | 3 | |
| α-helix | 324-336 | 13 | |
| α-helix | 343-345 | 3 | |
| β-strand | 346-351 | 6 | 8 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-363 | 9 | |
| β-strand | 369-373 | 5 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alcohol dehydrogenase E chain | A, B | protein | 374 | Equus caballus | P00327 (AlphaFold model) |
>6OWM_1 Alcohol dehydrogenase E chain (chains A, B) STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVTP LPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLWTPQCGKCRVCKHPEGNFCLKNDLSMPR GTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIGCGFSTGY GSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATEC VNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQN LSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVLPFEKINEGFD LLRSGESIRTILTF
| ID | Name | Formula | Copies |
|---|---|---|---|
| MRD | (4R)-2-methylpentane-2,4-diol | C6 H14 O2 | 3 |
| PFB | 2,3,4,5,6-pentafluorobenzyl alcohol | C7 H3 F5 O | 2 |
| NAJ | Nicotinamide-adenine-dinucleotide (acidic form) | C21 H27 N7 O14 P2 | 2 |
| ZN | Zinc ion | Zn | 4 |
Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen Transfer. Kim, K., Plapp, B.V. Biochemistry (2020) 59:862-879. DOI 10.1021/acs.biochem.9b01074 · PubMed
Other PDB entries of the same protein (UniProt P00327 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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