2A9U: Ubiquitin carboxyl-terminal hydrolase 8

Structure of the N-terminal domain of Human Ubiquitin carboxyl-terminal hydrolase 8 (USP8). Determined by X-ray diffraction at 2.1 Å resolution. Released 16 Aug 2005.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
2
Atoms
2,274
Mol. weight
34.05 kDa
Released
16 Aug 2005

Explore 2A9U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A9U contains 16 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: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix7-115
α-helix17-215
α-helix22-243
α-helix28-303
α-helix33-5220
α-helix56-7318
α-helix77-815
α-helix83-908
α-helix92-13847
Chain B: 7 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix17-226
α-helix28-303
α-helix33-5220
α-helix56-7318
α-helix77-804
α-helix83-908
α-helix92-13039

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin carboxyl-terminal hydrolase 8A, Bprotein144Homo sapiensP40818 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2A9U_1 Ubiquitin carboxyl-terminal hydrolase 8 (chains A, B)
GSMPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEER
AYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEV
RKKLEEKDRQEEAQRLQQKRQETG

Primary citation

Amino-terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-specific Protease 8 (USP8). Avvakumov, G.V., Walker, J.R., Xue, S. et al. J Biol Chem (2006) 281:38061-38070. DOI 10.1074/jbc.M606704200 · PubMed

Other PDB entries of the same protein (UniProt P40818 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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