2P2C: Caspase-2

Inhibition of caspase-2 by a designed ankyrin repeat protein (DARPin). Determined by X-ray diffraction at 3.24 Å resolution. Released 22 May 2007.

Method: X-ray diffraction
Resolution: 3.24 Å
Organism: Homo sapiens
Chains: 18
Atoms: 19,285
Mol. weight: 297.02 kDa
Released: 22 May 2007

Explore 2P2C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2P2C contains 106 α-helices and 86 β-strands across 18 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, 9 β-strands

Element	Residues	Length	Sheet
α-helix	16-20	5
α-helix	23-25	3
β-strand	26	1	1
β-strand	36-41	6	2
α-helix	57-70	14
β-strand	74-79	6	2
α-helix	83-95	13
α-helix	97-100	4
β-strand	105-110	6	2
β-strand	113-114	2	3
β-strand	117-119	3	3
β-strand	125-127	3	3
α-helix	128-133	6
α-helix	141-143	3
β-strand	148-153	6	2
β-strand	161	1	4

Chain B: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	210-211	2	5
β-strand	217-221	5	2
α-helix	238-250	13
α-helix	256-269	14
β-strand	283	1	4
β-strand	287-290	4	2
β-strand	295	1	1

Chain C: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	16-22	7
α-helix	23-25	3
β-strand	36-41	6	2
α-helix	57-70	14
β-strand	74-79	6	2
α-helix	83-95	13
α-helix	97-100	4
β-strand	105-110	6	2
β-strand	113-114	2	6
β-strand	117-119	3	6
β-strand	125-127	3	6
α-helix	128-133	6
α-helix	141-143	3
β-strand	148-152	5	2
β-strand	157	1	7
β-strand	164-165	2	5

Chain D: 2 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	217-221	5	2
β-strand	226	1	7
α-helix	238-250	13
α-helix	256-269	14
β-strand	287-290	4	2

Chain E: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	26	1	8
β-strand	36-41	6	9
α-helix	57-70	14
β-strand	74-79	6	9
α-helix	83-95	13
α-helix	97-100	4
β-strand	105-111	7	9
β-strand	113-114	2	10
β-strand	117-119	3	10
β-strand	125-127	3	10
α-helix	128-133	6
α-helix	141-143	3
β-strand	148-154	7	9
β-strand	157-159	3	11
β-strand	161	1	12
β-strand	164	1	13

Chain F: 2 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	210-211	2	14
β-strand	217-221	5	9
β-strand	226-227	2	11
α-helix	238-250	13
α-helix	256-269	14
β-strand	283	1	12
β-strand	287-290	4	9
β-strand	295	1	8

Chain G: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	16-22	7
α-helix	23-25	3
β-strand	26	1	15
β-strand	36-41	6	9
α-helix	57-70	14
β-strand	74-79	6	9
α-helix	83-95	13
α-helix	97-100	4
β-strand	105-110	6	9
β-strand	113-114	2	16
β-strand	117-119	3	16
β-strand	125-127	3	16
α-helix	128-133	6
α-helix	141-143	3
β-strand	148-153	6	9
β-strand	157	1	17
β-strand	161	1	18
β-strand	164-165	2	14

Chain H: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	211	1	13
β-strand	217-221	5	9
β-strand	226	1	17
β-strand	231-232	2	19
β-strand	236-237	2	19
α-helix	238-250	13
α-helix	256-269	14
β-strand	283	1	18
β-strand	287-290	4	9
β-strand	295	1	15

10 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Caspase-2	A, C, E, G, I, K	protein	169	Homo sapiens	P42575 (AlphaFold model)
Caspase-2	B, D, F, H, J, L	protein	106	Homo sapiens	P42575 (AlphaFold model)
Caspase-2	P, Q, R, S, T, U	protein	169	Homo sapiens

Sequence of entity 1 (A, C, E, G, I, K), FASTA

>2P2C_1 Caspase-2 (chains A, C, E, G, I, K)
MANKDGPLCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDV
DHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIY
GVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQD

Sequence of entity 2 (B, D, F, H, J, L), FASTA

>2P2C_2 Caspase-2 (chains B, D, F, H, J, L)
MAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADM
LVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT

Sequence of entity 3 (P, Q, R, S, T, U), FASTA

>2P2C_3 Caspase-2 (chains P, Q, R, S, T, U)
MRGSHHHHHHGSDLGKKLLEAARAGQDDEVRILMANGADVNATDWLGHTPLHLAAKTGHL
EIVEVLLKYGADVNAWDNYGATPLHLAADNGHLEIVEVLLKHGADVNAKDYEGFTPLHLA
AYDGHLEIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEILQKLN

Primary citation

Inhibition of Caspase-2 by a Designed Ankyrin Repeat Protein: Specificity, Structure, and Inhibition Mechanism. Schweizer, A., Roschitzki-Voser, H., Amstutz, P. et al. Structure (2007) 15:625-636. DOI 10.1016/j.str.2007.03.014 · 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
9C2Y 1.96 Å, Crystal Structure of JF1cpCasp2 in complex with MUR-65
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

Browse structure collections

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