4A3T: DNA mismatch repair protein HSM3

yeast regulatory particle proteasome assembly chaperone Hsm3. Determined by X-ray diffraction at 2.1 Å resolution. Released 11 Apr 2012.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
SACCHAROMYCES CEREVISIAE
Chains
2
Atoms
7,918
Mol. weight
112.03 kDa
Released
11 Apr 2012

Explore 4A3T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4A3T contains 80 α-helices and 0 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: 39 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix9-1911
α-helix29-4113
α-helix52-6312
α-helix73-8614
α-helix89-957
α-helix98-1058
α-helix110-12112
α-helix134-1429
α-helix150-16314
α-helix167-1715
α-helix172-1765
α-helix178-18710
α-helix190-20415
α-helix209-2113
α-helix214-2174
α-helix221-2288
α-helix231-25020
α-helix254-2563
α-helix257-2604
α-helix261-2633
α-helix264-2729
α-helix278-29518
α-helix300-30910
α-helix310-3145
α-helix320-3223
α-helix323-3297
α-helix332-3387
α-helix340-3467
α-helix354-3607
α-helix364-3685
α-helix371-3733
α-helix376-3816
α-helix384-39512
α-helix398-40710
α-helix409-4168
α-helix427-44115
α-helix445-4484
α-helix449-4513
α-helix452-46413
Chain B: 41 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix8-2013
α-helix29-4012
α-helix52-6312
α-helix66-683
α-helix73-8614
α-helix89-957
α-helix98-1069
α-helix110-12112
α-helix134-1429
α-helix150-16314
α-helix167-1715
α-helix172-1765
α-helix178-18710
α-helix190-20415
α-helix209-2113
α-helix214-2174
α-helix221-2288
α-helix231-25020
α-helix254-2563
α-helix257-2604
α-helix261-2633
α-helix264-2729
α-helix278-29518
α-helix304-3096
α-helix310-3145
α-helix320-3223
α-helix323-3297
α-helix332-3387
α-helix340-3467
α-helix354-3607
α-helix364-3685
α-helix371-3733
α-helix376-3816
α-helix384-39512
α-helix398-40710
α-helix409-4168
α-helix421-4233
α-helix427-44115
α-helix445-4484
α-helix449-4513
α-helix452-46413

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA mismatch repair protein HSM3A, Bprotein485SACCHAROMYCES CEREVISIAEP38348 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4A3T_1 DNA MISMATCH REPAIR PROTEIN HSM3 (chains A, B)
GAMADPSEKETNYVENLLTQLENELNEDNLPEDINTLLRKCSLNLVTVVSLPDMDVKPLL
ATIKRFLTSNVSYDSLNYDYLLDVVDKLVPMADFDDVLEVYSAEDLVKALRSEIDPLKVA
ACRVIENSQPKGLFATSNIIDILLDILFDEKVENDKLITAIEKALERLSTDELIRRRLFD
NNLPYLVSVKGRMETVSFVRLIDFLTIEFQFISGPEFKDIIFCFTKEEILKSVEDILVFI
ELVNYYTKFLLEIRNQDKYWALRHVKKILPVFAQLFEDTENYPDVRAFSTNCLLQLFAEV
SRIEEDEYSLFKTMDKDSLKIGSEAKLITEWLELINPQYLVKYHKDVVENYFHVSGYSIG
MLRNLSADEECFNAIRNKFSAEIVLRLPYLEQMQVVETLTRYEYTSKFLLNEMPKVMGSL
IGDGSAGAIIDLETVHYRNSALRNLLDKGEEKLSVWYEPLLREYSKAVNGKNYSTGSETK
IADCR

Primary citation

Dual Functions of the Hsm3 Protein in Chaperoning and Scaffolding Regulatory Particle Subunits During the Proteasome Assembly. Barrault, M.B., Richet, N., Godard, C. et al. Proc Natl Acad Sci U S A (2012) 109:E1001. DOI 10.1073/PNAS.1116538109 · PubMed

Other PDB entries of the same protein (UniProt P38348 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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