4LSZ: Caspase-7

Caspase-7 in Complex with DARPin D7.18. Determined by X-ray diffraction at 2.26 Å resolution. Released 2 Jul 2014.

Method
X-ray diffraction
Resolution
2.26 Å
Organisms
Homo sapiens, synthetic construct
Chains
6
Atoms
6,245
Mol. weight
100.94 kDa
Released
2 Jul 2014

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

Secondary structure: helices and β-sheets

4LSZ contains 40 α-helices and 38 β-strands across 6 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: 7 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand5911
β-strand66-7492
α-helix80-823
α-helix84-863
α-helix90-10415
β-strand106-11272
α-helix116-12712
β-strand134-14292
β-strand145-14623
β-strand149-15243
β-strand155-15843
α-helix159-1635
α-helix164-1663
α-helix172-1743
β-strand179-18462
β-strand19014
β-strand19215
β-strand195-19626
Chains B and D: 3 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand212-21327
β-strand219-22352
β-strand22914
β-strand233-23428
β-strand238-23928
α-helix240-25213
α-helix258-27215
α-helix280-2823
β-strand28615
β-strand290-29342
β-strand29811
Chain C: 6 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand5919
β-strand66-7492
α-helix80-823
α-helix90-10415
β-strand107-11262
α-helix116-12712
β-strand134-14292
β-strand145-146210
β-strand149-151310
β-strand156-158310
α-helix159-1635
α-helix164-1663
α-helix172-1743
β-strand179-18462
β-strand190111
β-strand192112
β-strand195-19627
Chain E: 10 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix13-2412
α-helix27-359
α-helix50-567
α-helix60-689
α-helix83-908
α-helix93-1019
α-helix116-1227
α-helix126-1349
α-helix149-1557
α-helix159-1635
Chain F: 11 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix14-2411
α-helix27-359
α-helix50-567
α-helix60-689
α-helix83-908
α-helix93-1019
α-helix116-1227
α-helix126-1349
α-helix141-1433
α-helix149-1557
α-helix159-1657

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Caspase-7 subunit p20A, Cprotein175Homo sapiensP55210 (AlphaFold model)
Caspase-7 subunit p10B, Dprotein105Homo sapiensP55210 (AlphaFold model)
DARPin D7.18E, Fprotein169synthetic construct
Sequence of entity 1 (A, C), FASTA
>4LSZ_1 Caspase-7 subunit p20 (chains A, C)
AKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTG
MGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLS
HGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQAD
Sequence of entity 2 (B, D), FASTA
>4LSZ_2 Caspase-7 subunit p10 (chains B, D)
ANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVN
DRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQLEHHHHHH
Sequence of entity 3 (E, F), FASTA
>4LSZ_3 DARPin D7.18 (chains E, F)
MRGSHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNADDAWGQTPLHLAAQNGHL
EIVEVLLKHDADVNATDWVGMTPLHLAADDGHLEIVEALLKYGADVNAYDQLGNTPLNLA
ATDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN

Primary citation

Combined inhibition of caspase 3 and caspase 7 by two highly selective DARPins slows down cellular demise. Flutsch, A., Ackermann, R., Schroeder, T. et al. Biochem J (2014) 461:279-290. DOI 10.1042/BJ20131456 · PubMed

Other PDB entries of the same protein (UniProt P55210 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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