2AR9: Dimeric caspase-9

Crystal structure of a dimeric caspase-9. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Oct 2005.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,286
Mol. weight: 122.35 kDa
Ligands: MLT
Released: 11 Oct 2005

Explore 2AR9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2AR9 contains 34 α-helices and 52 β-strands across 4 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: 11 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	141-146	6
β-strand	152-153	2	1
β-strand	161-167	7	2
α-helix	173-175	3
α-helix	177-179	3
α-helix	183-196	14
β-strand	199-205	7	2
α-helix	209-220	12
α-helix	224-226	3
β-strand	229-235	7	2
β-strand	238-239	2	3
β-strand	243	1	4
β-strand	249-251	3	3
β-strand	257-259	3	3
α-helix	260-265	6
α-helix	273-275	3
β-strand	280-285	6	2
β-strand	341-345	5	2
α-helix	362-374	13
α-helix	380-391	12
α-helix	398-399	2
β-strand	402-405	4	2
β-strand	410-411	2	1

Chains B and D: 8 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	141-147	7
β-strand	152	1	5
β-strand	161-167	7	2
α-helix	183-196	14
β-strand	199-205	7	2
α-helix	209-221	13
α-helix	224-226	3
β-strand	230-235	6	2
β-strand	238	1	6
β-strand	243	1	4
β-strand	249-251	3	6
β-strand	257-259	3	6
α-helix	260-266	7
α-helix	273-275	3
β-strand	280-285	6	2
β-strand	341-346	6	2
β-strand	351	1	7
β-strand	361	1	7
α-helix	362-374	13
α-helix	380-394	15
β-strand	402-405	4	2
β-strand	410	1	5

Chain C: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	143-147	5
β-strand	152-153	2	8
β-strand	161-167	7	9
α-helix	184-196	13
β-strand	199-205	7	9
α-helix	209-219	11
β-strand	230-235	6	9
β-strand	238-239	2	10
β-strand	243	1	11
β-strand	249-251	3	10
β-strand	257-259	3	10
α-helix	260-266	7
α-helix	273-275	3
β-strand	280-285	6	9
β-strand	341-345	5	9
α-helix	362-372	11
α-helix	380-393	14
β-strand	402-405	4	9
β-strand	410-411	2	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Caspase-9	A, B, C, D	protein	278	Homo sapiens	P55211 (AlphaFold model)

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

>2AR9_1 Caspase-9 (chains A, B, C, D)
MGALESLRGNADLAYILSMEPCGHCLIINNVNFCRESGLRTRTGSNIDCEKLRRRFSSLH
FMVEVKGDLTAKKMVLALLELARQDHGALDCCVVVILSHGCQASHLQFPGAVYGTDGCPV
SVEKIVNIFNGTSCPSLGGKPKLFFIQASGGEQKDHGFEVASTSPEDESPGSNPEPDATP
FQEGLRTFDQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSE
DLQSLLLRVANAVSVKGIYKQMPCIVSMLRKKLFFKTS

Ligands and cofactors

ID	Name	Formula	Copies
MLT	D-malate	C4 H6 O5	1

Primary citation

Engineering a Dimeric Caspase-9: A Re-Evaluation of the Induced Proximity Model for Caspase Activation. Chao, Y., Shiozaki, E.N., Srinivassula, S.M. et al. PLoS Biol (2005) 3:1079-1087. DOI 10.1371/journal.pbio.0030183 · PubMed

Other PDB entries of the same protein (UniProt P55211 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3D9T 1.5 Å, CIAP1-BIR3 in complex with N-terminal peptide from Caspase-9 (ATPFQE)
4RHW 2.1 Å, Crystal structure of Apaf-1 CARD and caspase-9 CARD complex
1NW9 2.4 Å, Structure of caspase-9 in an inhibitory complex with xiap-BIR3
9R44 2.46 Å, Crystal structure of human caspase-9 CARD
3YGS 2.5 Å, Apaf-1 card in complex with prodomain of procaspase-9
1JXQ 2.8 Å, Structure of cleaved, CARD domain deleted Caspase-9
5WVC 2.99 Å, Structure of the CARD-CARD disk
9S6F 3.3 Å, Cryo-EM structure of human caspase-9 CARD (WT) filament
3V3K 3.49 Å, Human caspase 9 in complex with bacterial effector protein
9S6E 3.5 Å, Cryo-EM structure of human caspase-9 CARD (H38R) mutant filament
5JUY 4.1 Å, Active human apoptosome with procaspase-9
5WVE 4.4 Å, Apaf-1-Caspase-9 holoenzyme

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