Structure for peptidase C14.006: caspase-2

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

 

PDB Organism Resolution Comment
1PYO_A Homo sapiens 1.65 Å complex with acetyl-Leu-Asp-Glu-Ser-Asp-CHO
One molecule of the dimer is shown. Catalytic residues are shown in ball-and-stick representation: His260 in purple and Cys303 in yellow. Bound inhibitor is shown in grey in ball-and-stick representation.
This browser does not have a Java Plug-in.
Get the latest Java Plug-in here.
Show surface
TERTIARY STRUCTURE DATA
Comment Resolution PDB PDBe SCOP CATH PDBSum Proteopedia Reference
Homo sapiens
complex with acetyl-Leu-Asp-Glu-Ser-Asp-CHO 1.65 Å 1PYO 1PYO 1PYO 1PYO 1PYO 1PYO Schweizer et al., 2003
inhibition of caspase-2 by a designed ankyrin repeat protein (darpin) 3.24 Å 2P2C 2P2C 2P2C 2P2C 2P2C 2P2C Schweizer et al., 2007
crystal structure of active caspase-2 bound with ac-advad-cho 1.77 Å 3R5J 3R5J 3R5J 3R5J 3R5J 3R5J
crystal structure of active caspase-2 bound with ac-vdvad-cho 2.07 Å 3R6G 3R6G 3R6G 3R6G 3R6G 3R6G
caspase-2 t380a bound with ac-vdvad-cho 1.90 Å 3R6L 3R6L 3R6L 3R6L 3R6L 3R6L
complex with one molecule of Ac-DVAD-CHO 1.80 Å 3R7B 3R7B 3R7B 3R7B 3R7B 3R7B
complex with two molecules of Ac-DVAD-CHO 2.33 Å 3R7N 3R7N 3R7N 3R7N 3R7N 3R7N
crystal structure of apo caspase2 2.25 Å 3R7S 3R7S 3R7S 3R7S 3R7S 3R7S
complex with chdi ligand 33c 2.55 Å 3RJM 3RJM 3RJM 3RJM 3RJM 3RJM