9C2Y: JF1cpCasp2

Crystal Structure of JF1cpCasp2 in complex with MUR-65. Determined by X-ray diffraction at 1.96 Å resolution. Released 9 Apr 2025.

Method: X-ray diffraction
Resolution: 1.96 Å
Organisms: Homo sapiens, synthetic construct
Chains: 8
Atoms: 7,701
Mol. weight: 129.53 kDa
Released: 9 Apr 2025

Explore 9C2Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9C2Y contains 31 α-helices and 76 β-strands across 8 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, 17 β-strands

Element	Residues	Length	Sheet
β-strand	32	1	1
β-strand	38-42	5	2
β-strand	51-53	3	3
β-strand	57-58	2	3
α-helix	59-71	13
α-helix	77-90	14
β-strand	104	1	4
β-strand	108-111	4	2
β-strand	116	1	5
β-strand	140	1	5
β-strand	149-155	7	2
α-helix	171-184	14
β-strand	188-193	6	2
α-helix	197-209	13
α-helix	211-215	5
β-strand	218-224	7	2
β-strand	227-228	2	6
β-strand	231-233	3	6
β-strand	239-241	3	6
α-helix	242-247	6
α-helix	255-257	3
β-strand	262-267	6	2
β-strand	275	1	4
β-strand	278	1	7

Chain B: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	32	1	7
β-strand	38-42	5	2
β-strand	47	1	8
β-strand	51-53	3	9
β-strand	57-58	2	9
α-helix	59-71	13
α-helix	77-90	14
β-strand	104	1	10
β-strand	108-111	4	2
β-strand	116	1	11
α-helix	126-129	4
α-helix	130-136	7
α-helix	137-139	3
β-strand	140	1	11
β-strand	149-155	7	2
α-helix	171-185	15
β-strand	187-193	7	2
α-helix	197-209	13
α-helix	211-214	4
β-strand	218-224	7	2
β-strand	227-228	2	12
β-strand	231-233	3	12
β-strand	239-241	3	12
α-helix	242-247	6
α-helix	255-257	3
β-strand	262-267	6	2
β-strand	271	1	8
β-strand	275	1	10
β-strand	278	1	1

Chain C: 7 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	31-32	2	13
β-strand	38-42	5	14
β-strand	51-53	3	15
β-strand	57-58	2	15
α-helix	59-71	13
α-helix	77-90	14
β-strand	104	1	16
β-strand	108-111	4	14
β-strand	116	1	17
β-strand	140	1	17
β-strand	149-155	7	14
α-helix	171-184	14
β-strand	187-193	7	14
α-helix	197-208	12
α-helix	211-215	5
β-strand	218-224	7	14
β-strand	227-228	2	18
β-strand	231-233	3	18
β-strand	239-241	3	18
α-helix	242-248	7
α-helix	255-257	3
β-strand	262-267	6	14
β-strand	275	1	16
β-strand	278-279	2	19

Chain D: 7 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	31-32	2	19
β-strand	38-42	5	14
β-strand	48	1	20
β-strand	51-53	3	21
β-strand	57-58	2	21
α-helix	59-71	13
α-helix	77-90	14
β-strand	104	1	22
β-strand	108-111	4	14
β-strand	116	1	23
β-strand	140	1	23
β-strand	149-155	7	14
α-helix	171-184	14
β-strand	187-193	7	14
α-helix	197-209	13
α-helix	211-214	4
β-strand	218-224	7	14
β-strand	227-228	2	24
β-strand	231-233	3	24
β-strand	239-241	3	24
α-helix	242-247	6
α-helix	255-257	3
β-strand	262-267	6	14
β-strand	273	1	20
β-strand	275	1	22
β-strand	278-279	2	13

Chains F, G, H and I: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	2-4	3	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
JF1cpCasp2	A, B, C, D	protein	282	Homo sapiens	P42575 (AlphaFold model)
MUR-65	F, G, H, I	protein	5	synthetic construct

Sequence of entity 1 (A, B, C, D), FASTA

>9C2Y_1 JF1cpCasp2 (chains A, B, C, D)
MHHHHHHGKNHAGSPGCEESAAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWY
IEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLF
PGGGVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVT
LFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLL
QLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQD

Sequence of entity 2 (F, G, H, I), FASTA

>9C2Y_2 MUR-65 (chains F, G, H, I)
XXVXX

Primary citation

Reengineering of Circularly Permuted Caspase-2 to Enhance Enzyme Stability and Enable Crystallographic Studies. Fuller, J.L., Shi, K., Pockes, S. et al. ACS Chem Biol (2025) 20:845-857. DOI 10.1021/acschembio.4c00795 · PubMed

Other PDB entries of the same protein (UniProt P42575 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6Y8D 1.51 Å, 14-3-3 Sigma in complex with phosphorylated caspase{pS164} peptide
8VP4 1.51 Å, Crystal Structure of JF1cpCasp2 with Peptide Inhibitor AcVDVAD-CHO
6Y8B 1.54 Å, 14-3-3 Sigma in complex with phosphorylated caspase{pS139} peptide
6S9K 1.6 Å, Structure of 14-3-3 gamma in complex with caspase-2 peptide containing 14-3-3 binding…
1PYO 1.65 Å, Crystal Structure of Human Caspase-2 in Complex with Acetyl-Leu-Asp-Glu-Ser-Asp-cho
3R5J 1.77 Å, Crystal structure of active caspase-2 bound with Ac-ADVAD-CHO
3R7B 1.8 Å, Caspase-2 bound to one copy of Ac-DVAD-CHO
3R6L 1.9 Å, Caspase-2 T380A bound with Ac-VDVAD-CHO
3R6G 2.07 Å, Crystal structure of active caspase-2 bound with Ac-VDVAD-CHO
3R7S 2.25 Å, Crystal Structure of Apo Caspase2
3R7N 2.33 Å, Caspase-2 bound with two copies of Ac-DVAD-CHO
3RJM 2.55 Å, CASPASE2 in complex with chdi ligand 33c

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