4M92: HN33/Tusc3-peptide 2

Crystal structure of hN33/Tusc3-peptide 2. Determined by X-ray diffraction at 1.6 Å resolution. Released 26 Mar 2014.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Homo sapiens
Chains
2
Atoms
1,581
Mol. weight
20.96 kDa
Released
26 Mar 2014

Explore 4M92 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4M92 contains 10 α-helices and 7 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: 10 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix3-2119
β-strand25-2621
α-helix29-324
α-helix33-375
α-helix401
β-strand44-5071
α-helix54-563
α-helix59-7719
β-strand85-9171
α-helix96-1016
β-strand10612
β-strand109-11351
α-helix121-1233
β-strand12411
α-helix127-1304
α-helix134-14512
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand1112

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tumor suppressor candidate 3Aprotein161Homo sapiensQ13454 (AlphaFold model)
Interleukin-1 receptor accessory protein-like 1Bprotein16Homo sapiensQ9NZN1 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4M92_1 Tumor suppressor candidate 3 (chains A)
ASKKENLLAEKVEQLMEWSSRRSIFRMNGDKFRKFIKAPPRNYSMIVMFTALQPQRQCSV
SRQANEEYQILANSWRYSSAFSNKLFFSMVDYDEGTDVFQQLNMNSAPTFMHFPPKGRPK
RADTFDLQRIGFAAEQLAKWIADRTDVHIRVFRLEHHHHHH
Sequence of entity 2 (B), FASTA
>4M92_2 Interleukin-1 receptor accessory protein-like 1 (chains B)
REDDIGNYTCELKYGG

Primary citation

Structural basis of substrate specificity of human oligosaccharyl transferase subunit n33/tusc3 and its role in regulating protein N-glycosylation. Mohorko, E., Owen, R.L., Malojcic, G. et al. Structure (2014) 22:590-601. DOI 10.1016/j.str.2014.02.013 · PubMed

Other PDB entries of the same protein (UniProt Q13454 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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