1ERV: Thioredoxin

Human thioredoxin mutant with cys 73 replaced by ser (reduced form). Determined by X-ray diffraction at 1.65 Å resolution. Released 14 Oct 1996.

Method
X-ray diffraction
Resolution
1.65 Å
Organism
Homo sapiens
Chains
1
Atoms
880
Mol. weight
11.73 kDa
Released
14 Oct 1996

Explore 1ERV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ERV contains 4 α-helices and 5 β-strands across 1 chain. 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: 4 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand3-531
α-helix8-1710
β-strand23-2861
α-helix33-4816
β-strand53-5861
α-helix63-686
β-strand76-8161
β-strand84-9071
α-helix94-10411

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ThioredoxinAprotein105Homo sapiensP10599 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1ERV_1 THIOREDOXIN (chains A)
MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVD
DCQDVASECEVKSMPTFQFFKKGQKVGEFSGANKEKLEATINELV

Primary citation

Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Weichsel, A., Gasdaska, J.R., Powis, G. et al. Structure (1996) 4:735-751. DOI 10.1016/S0969-2126(96)00079-2 · PubMed

Other PDB entries of the same protein (UniProt P10599 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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