6OWM: Horse liver F93W alcohol dehydrogenase

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.

Method
X-ray diffraction
Resolution
1.1 Å
Organism
Equus caballus
Chains
2
Atoms
7,165
Mol. weight
82.12 kDa
Ligands
MRD, PFB, NAJ, ZN
Released
22 May 2019

Explore 6OWM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 22 helices, 22 β-strands

ElementResiduesLengthSheet
α-helix61
β-strand7-1481
β-strand22-2871
α-helix29-313
β-strand35-44102
α-helix47-548
β-strand63-6421
β-strand68-7692
β-strand88-9142
α-helix101-1044
β-strand130-13231
β-strand135-13841
β-strand14711
β-strand149-15352
α-helix154-1563
β-strand157-15932
α-helix166-1694
α-helix170-1734
α-helix175-1817
α-helix182-1876
β-strand194-19853
α-helix202-21312
β-strand218-22253
α-helix226-2283
α-helix229-2357
β-strand239-24133
α-helix243-2453
α-helix250-2578
β-strand26214
β-strand264-26743
α-helix272-28110
β-strand28214
β-strand288-29143
α-helix299-3002
β-strand301-30335
α-helix306-3094
β-strand313-31643
α-helix319-3213
α-helix324-33613
α-helix343-3453
β-strand346-35162
α-helix352-3543
α-helix355-3639
β-strand369-37352
Chain B: 23 helices, 24 β-strands
ElementResiduesLengthSheet
α-helix61
β-strand7-1376
β-strand1417
α-helix20-212
β-strand22-2876
α-helix29-313
β-strand35-44108
α-helix47-548
β-strand6317
β-strand69-7688
β-strand88-9148
α-helix101-1044
β-strand130-13236
β-strand135-13736
β-strand13817
β-strand14716
β-strand149-15358
α-helix154-1563
β-strand157-15938
α-helix166-1694
α-helix170-1734
α-helix175-1817
α-helix182-1876
α-helix189-1902
β-strand194-19853
α-helix202-21312
β-strand218-22253
α-helix226-2283
α-helix229-2357
β-strand239-24133
α-helix243-2453
α-helix250-2578
β-strand26219
β-strand264-26743
α-helix272-28110
β-strand28219
β-strand288-29143
β-strand301-30335
α-helix306-3094
β-strand313-31643
α-helix319-3213
α-helix324-33613
α-helix343-3453
β-strand346-35168
α-helix352-3543
α-helix355-3639
β-strand369-37358

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alcohol dehydrogenase E chainA, Bprotein374Equus caballusP00327 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6OWM_1 Alcohol dehydrogenase E chain (chains A, B)
STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVTP
LPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLWTPQCGKCRVCKHPEGNFCLKNDLSMPR
GTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIGCGFSTGY
GSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATEC
VNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQN
LSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVLPFEKINEGFD
LLRSGESIRTILTF

Ligands and cofactors

IDNameFormulaCopies
MRD(4R)-2-methylpentane-2,4-diolC6 H14 O23
PFB2,3,4,5,6-pentafluorobenzyl alcoholC7 H3 F5 O2
NAJNicotinamide-adenine-dinucleotide (acidic form)C21 H27 N7 O14 P22
ZNZinc ionZn4

Primary citation

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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