1JXQ: Cleaved, CARD domain deleted Caspase-9

Structure of cleaved, CARD domain deleted Caspase-9. Determined by X-ray diffraction at 2.8 Å resolution. Released 12 Dec 2001.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Homo sapiens
Chains
6
Atoms
7,596
Mol. weight
126.79 kDa
Released
12 Dec 2001

Explore 1JXQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1JXQ contains 33 α-helices and 70 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: 9 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix141-1477
β-strand152-15321
β-strand163-16972
α-helix176-1783
α-helix182-19514
β-strand198-20472
α-helix208-21912
β-strand229-23572
β-strand238-23923
β-strand240C14
β-strand242-24433
β-strand255-25733
α-helix258-2647
α-helix271-2733
β-strand278-28362
β-strand28915
β-strand29116
β-strand294-29527
β-strand327-33152
β-strand33715
α-helix338-3392
β-strand34018
α-helix348-36013
α-helix366-37813
β-strand38416
β-strand388-39352
β-strand397-39821
Chain B: 7 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand15219
β-strand163-16972
α-helix176-1783
α-helix182-19514
β-strand198-20472
α-helix208-21912
β-strand229-23682
β-strand238110
β-strand240C14
β-strand242-244310
β-strand255-257310
α-helix258-2636
α-helix271-2733
β-strand278-28472
β-strand320-32127
β-strand327-33262
β-strand337111
β-strand347111
α-helix348-36013
α-helix366-38015
β-strand388-39352
β-strand39719
Chain C: 10 helices, 20 β-strands
ElementResiduesLengthSheet
α-helix141-1477
β-strand152-153212
β-strand163-169713
α-helix176-1783
α-helix182-19514
β-strand198-204713
α-helix208-22013
β-strand229-235713
β-strand238-239214
β-strand240C115
β-strand242-244314
β-strand255-257314
α-helix258-2636
α-helix271-2733
β-strand278-283613
β-strand289116
β-strand291117
β-strand294-295218
β-strand327-331513
β-strand337116
α-helix338-3392
β-strand340119
β-strand341-342220
β-strand346-347220
α-helix348-36013
α-helix366-37712
β-strand384117
β-strand388-393513
β-strand397-398212
α-helix400-4023
Chain D: 7 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand152121
β-strand163-169713
α-helix176-1783
α-helix182-19514
β-strand198-204713
α-helix208-21912
β-strand229-236813
β-strand238122
β-strand240C115
β-strand242-244322
β-strand255-257322
α-helix258-2636
α-helix271-2733
β-strand278-284713
β-strand320-321218
β-strand327-332613
β-strand337-339323
β-strand342-347623
α-helix348-36013
α-helix366-37813
β-strand388-393513
β-strand397121
Chains E and F: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand50418

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Caspase-9A, B, C, Dprotein284Homo sapiensP55211 (AlphaFold model)
benzoxycarbonyl-Val-Ala-Asp-fluoromethyl ketone InhibitorE, Fprotein5
Sequence of entity 1 (A, B, C, D), FASTA
>1JXQ_1 Caspase-9 (chains A, B, C, D)
MGALESLRGNADLAYILSMEPCGHCLIINNVNFCRESGLRTRTGSNIDCEKLRRRFSSLH
FMVEVKGDLTAKKMVLALLELARQDHGALDCCVVVILSHGCQASHLQFPGAVYGTDGCPV
SVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATP
FQEGLRTFDQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSE
DLQSLLLRVANAVSVKGIYKQMPGCFNFLRKKLFFKTSHHHHHH
Sequence of entity 2 (E, F), FASTA
>1JXQ_2 benzoxycarbonyl-Val-Ala-Asp-fluoromethyl ketone Inhibitor (chains E, F)
XEVDX

Primary citation

Dimer formation drives the activation of the cell death protease caspase 9. Renatus, M., Stennicke, H.R., Scott, F.L. et al. Proc Natl Acad Sci U S A (2001) 98:14250-14255. DOI 10.1073/pnas.231465798 · PubMed

Other PDB entries of the same protein (UniProt P55211 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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