5TXK: USP35 C450S

Crystal structure of USP35 C450S in complex with ubiquitin. Determined by X-ray diffraction at 1.84 Å resolution. Released 9 May 2018.

Method
X-ray diffraction
Resolution
1.84 Å
Organism
Homo sapiens
Chains
2
Atoms
3,875
Mol. weight
50.86 kDa
Ligands
ZN
Released
9 May 2018

Explore 5TXK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5TXK contains 16 α-helices and 29 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: 12 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand442-44321
α-helix450-46112
α-helix463-4708
α-helix479-49315
β-strand498-49921
α-helix502-5076
α-helix5141
β-strand51912
α-helix521-54929
α-helix565-5706
β-strand572-58093
β-strand586-59383
β-strand596-59834
α-helix599-6024
β-strand76015
α-helix761-7688
β-strand772-77433
α-helix776-7783
β-strand780-78236
β-strand787-78936
β-strand791-79993
β-strand803-80864
β-strand811-81447
β-strand819-82247
β-strand82815
β-strand832-83654
α-helix838-8403
β-strand842-854134
β-strand862-86764
β-strand891-89444
β-strand897-90044
α-helix903-91210
β-strand916-925104
Chain B: 4 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand2-658
β-strand12-1658
β-strand2219
α-helix23-3412
α-helix38-403
β-strand42-4548
β-strand48-4928
α-helix50-512
β-strand5519
α-helix57-593
β-strand66-7058
β-strand7512

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin carboxyl-terminal hydrolase 35,Ubiquitin carboxyl-terminal hydrolase 35Aprotein372Homo sapiensQ9P2H5 (AlphaFold model)
Polyubiquitin-BBprotein76Homo sapiensP0CG47 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5TXK_1 Ubiquitin carboxyl-terminal hydrolase 35,Ubiquitin carboxyl-terminal hydrolase 35 (chains A)
SELAGFYPRLMAKSDTGKIGLINLGNTSYVNSILQALFMASDFRHCVLRLTENNSQPLMT
KLQWLFGFLEHSQRPAISPENFLSASWTPWFSPGTQQDCSEYLKYLLDRLHEEEKTGTRI
CQKLKQSSSPSPPEEPPAPSSTSVEKMFGGKIVTRICCLCCLNVSSREEAFTDLSLAFPP
PGSEGSRSVLDLVNYFLSPEKLTAENRYYCESCASLQDAEKVVELSQGPCYLILTLLRFS
FDLRTMRRRKILDDVSIPLLLRLPLAGGRGQAYDLCSVVVHSGVSSESGHYYCYAREGAA
RPAASLGTADRPEPENQWYLFNDTRVSFSSFESVSNVTSFFPKDTAYVLFYRQRPREGPE
AELGSSRVRTEP
Sequence of entity 2 (B), FASTA
>5TXK_2 Polyubiquitin-B (chains B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Water and common crystallization additives (EDO, SO4) are not listed.

Primary citation

Expansion of DUB functionality generated by alternative isoforms - USP35, a case study. Leznicki, P., Natarajan, J., Bader, G. et al. J Cell Sci (2018) 131. DOI 10.1242/jcs.212753 · PubMed

Other PDB entries of the same protein (UniProt Q9P2H5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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