2ZNR: DUB domain of human AMSH-LP

Crystal structure of the DUB domain of human AMSH-LP. Determined by X-ray diffraction at 1.2 Å resolution. Released 2 Sept 2008.

Method
X-ray diffraction
Resolution
1.2 Å
Organism
Homo sapiens
Chains
1
Atoms
1,732
Mol. weight
20.68 kDa
Ligands
ZN, PR
Released
2 Sept 2008

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

Secondary structure: helices and β-sheets

2ZNR contains 7 α-helices and 11 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: 7 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix266-2683
β-strand269-27241
α-helix275-28713
β-strand294-30291
β-strand305-31391
β-strand316-31942
β-strand322-32542
α-helix328-33811
β-strand341-34881
α-helix3531
α-helix358-37013
β-strand375-38061
α-helix381-3833
β-strand385-39171
α-helix393-4019
β-strand417-41931
β-strand423-42641
β-strand431-43441

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AMSH-like proteaseAprotein178Homo sapiensQ96FJ0 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2ZNR_1 AMSH-like protease (chains A)
GPGHMEGLRCVVLPEDLCHKFLQLAESNTVRGIETCGILCGKLTHNEFTITHVIVPKQSA
GPDYCDMENVEELFNVQDQHDLLTLGWIHTHPTQTAFLSSVDLHTHCSYQLMLPEAIAIV
CSPKHKDTGIFRLTNAGMLEVSACKKKGFHPHTKEPRLFSICKHVLVKDIKIIVLDLR

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
PRPraseodymium ionPr1

Water and common crystallization additives (EDO) are not listed.

Primary citation

Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains. Sato, Y., Yoshikawa, A., Yamagata, A. et al. Nature (2008) 455:358-362. DOI 10.1038/nature07254 · PubMed

Other PDB entries of the same protein (UniProt Q96FJ0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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