3R7N: Caspase-2

Caspase-2 bound with two copies of Ac-DVAD-CHO. Determined by X-ray diffraction at 2.33 Å resolution. Released 27 Jul 2011.

Method: X-ray diffraction
Resolution: 2.33 Å
Organism: Homo sapiens
Chains: 6
Atoms: 4,280
Mol. weight: 62.89 kDa
Released: 27 Jul 2011

Explore 3R7N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3R7N contains 23 α-helices and 40 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, 11 β-strands

Element	Residues	Length	Sheet
α-helix	177-180	4
α-helix	181-187	7
α-helix	188-190	3
β-strand	191	1	1
β-strand	200-206	7	2
α-helix	222-235	14
β-strand	238-244	7	2
α-helix	248-259	12
α-helix	262-265	4
β-strand	269-275	7	2
β-strand	278-279	2	3
β-strand	282-284	3	3
β-strand	290-292	3	3
α-helix	293-299	7
α-helix	306-308	3
β-strand	313-318	6	2
β-strand	324	1	4
α-helix	325	1
β-strand	326	1	5
β-strand	329	1	6

Chain B: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	357-358	2	7
β-strand	364-368	5	2
β-strand	374	1	4
β-strand	377-379	3	8
β-strand	383-384	2	8
α-helix	385-397	13
α-helix	403-416	14
β-strand	430	1	5
β-strand	434-437	4	2
β-strand	442	1	1

Chain C: 9 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	177-180	4
α-helix	181-187	7
α-helix	188-190	3
β-strand	191	1	9
β-strand	200-206	7	2
α-helix	222-235	14
β-strand	238-244	7	2
α-helix	248-260	13
α-helix	262-266	5
β-strand	269-275	7	2
β-strand	278-279	2	10
β-strand	282-284	3	10
β-strand	290-292	3	10
α-helix	293-298	6
α-helix	306-308	3
β-strand	313-318	6	2
β-strand	324	1	11
β-strand	326	1	12
β-strand	329-330	2	7
α-helix	331-332	2

Chain D: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	358	1	6
β-strand	364-368	5	2
β-strand	374	1	11
α-helix	375-376	2
β-strand	377-379	3	13
β-strand	383-384	2	13
α-helix	385-397	13
α-helix	403-416	14
β-strand	430	1	12
β-strand	434-437	4	2
β-strand	442	1	9

Chains E and F: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	404-405	2	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Caspase-2 subunit p18	A, C	protein	160	Homo sapiens	P42575 (AlphaFold model)
Caspase-2 subunit p12	B, D	protein	112	Homo sapiens	P42575 (AlphaFold model)
Peptide Inhibitor (ACE)DVAD-CHO	E, F	protein	5

Sequence of entity 1 (A, C), FASTA

>3R7N_1 Caspase-2 subunit p18 (chains A, C)
MQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLF
KLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQL
QEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQD

Sequence of entity 2 (B, D), FASTA

>3R7N_2 Caspase-2 subunit p12 (chains B, D)
GKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLV
KVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPTLEHHHHHH

Sequence of entity 3 (E, F), FASTA

>3R7N_3 Peptide Inhibitor (ACE)DVAD-CHO (chains E, F)
XDVAD

Primary citation

Structural and enzymatic insights into caspase-2 protein substrate recognition and catalysis. Tang, Y., Wells, J.A., Arkin, M.R. J Biol Chem (2011) 286:34147-34154. DOI 10.1074/jbc.M111.247627 · 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
3RJM 2.55 Å, CASPASE2 in complex with chdi ligand 33c

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