3R6L: Caspase-2 T380A
Caspase-2 T380A bound with Ac-VDVAD-CHO. Determined by X-ray diffraction at 1.9 Å resolution. Released 27 Jul 2011.
- Method
- X-ray diffraction
- Resolution
- 1.9 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 4,489
- Mol. weight
- 63.02 kDa
- Released
- 27 Jul 2011
Explore 3R6L in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3R6L contains 22 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: 8 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 |
| β-strand | 326 | 1 | 5 |
| β-strand | 329-330 | 2 | 6 |
Chain B: 3 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 |
| α-helix | 375-376 | 2 | |
| 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 | 248-259 | 12 | |
| 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 | 293-299 | 7 | |
| 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: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 357-358 | 2 | 6 |
| β-strand | 364-368 | 5 | 2 |
| β-strand | 374 | 1 | 11 |
| 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 |
Chain E: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 403-405 | 3 | 8 |
Chain F: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 404-405 | 2 | 13 |
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)VDVAD-CHO | E, F | protein | 6 | | |
Sequence of entity 1 (A, C), FASTA
>3R6L_1 Caspase-2 subunit p18 (chains A, C)
MQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLF
KLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQL
QEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQD
Sequence of entity 2 (B, D), FASTA
>3R6L_2 Caspase-2 subunit p12 (chains B, D)
GKEKLPKMRLPTRSDMICGYACLKGTAAMRNAKRGSWYIEALAQVFSERACDMHVADMLV
KVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPTLEHHHHHH
Sequence of entity 3 (E, F), FASTA
>3R6L_3 Peptide Inhibitor (ACE)VDVAD-CHO (chains E, F)
XVDVAD
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
- 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
- 3RJM 2.55 Å, CASPASE2 in complex with chdi ligand 33c
Browse structure collections
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