4RHW: Apaf-1 CARD and caspase-9 CARD complex

Crystal structure of Apaf-1 CARD and caspase-9 CARD complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 15 Oct 2014.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 6
Atoms: 4,976
Mol. weight: 70.63 kDa
Released: 15 Oct 2014

Explore 4RHW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4RHW contains 43 α-helices and 0 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, 0 β-strands

Element	Residues	Length
α-helix	3-11	9
α-helix	13-19	7
α-helix	22-24	3
α-helix	26-31	6
α-helix	37-44	8
α-helix	49-60	12
α-helix	65-77	13
α-helix	81-88	8
α-helix	91-93	3

Chains B and D: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	3-19	17
α-helix	22-32	11
α-helix	37-45	9
α-helix	49-61	13
α-helix	65-77	13
α-helix	81-88	8

Chain C: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	3-11	9
α-helix	13-19	7
α-helix	22-24	3
α-helix	26-32	7
α-helix	37-44	8
α-helix	49-61	13
α-helix	65-77	13
α-helix	81-88	8

Chain E: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	3-11	9
α-helix	13-19	7
α-helix	26-31	6
α-helix	37-44	8
α-helix	51-62	12
α-helix	69-79	11
α-helix	83-93	11

Chain F: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	3-11	9
α-helix	13-19	7
α-helix	26-31	6
α-helix	37-44	8
α-helix	51-62	12
α-helix	69-79	11
α-helix	83-94	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apoptotic protease-activating factor 1	A, B, C, D	protein	97	Homo sapiens	O14727 (AlphaFold model)
Caspase-9	E, F	protein	108	Homo sapiens	P55211 (AlphaFold model)

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

>4RHW_1 Apoptotic protease-activating factor 1 (chains A, B, C, D)
MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI
LKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSS

Sequence of entity 2 (E, F), FASTA

>4RHW_2 Caspase-9 (chains E, F)
MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMIEDIQRAGSGSRRDQARQLII
DLETRGSQALPLFISCLEDTGQDMLASFLRTNRQAAKLSKLEHHHHHH

Primary citation

Molecular determinants of caspase-9 activation by the Apaf-1 apoptosome. Hu, Q., Wu, D., Chen, W. et al. Proc Natl Acad Sci U S A (2014) 111:16254-16261. DOI 10.1073/pnas.1418000111 · PubMed

Other PDB entries of the same protein (UniProt O14727 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1CY5 1.3 Å, Crystal structure of the apaf-1 card
2P1H 1.59 Å, Rapid Folding and Unfolding of Apaf-1 CARD
2YGS 1.6 Å, Card domain from apaf-1
1Z6T 2.21 Å, Structure of the apoptotic protease-activating factor 1 bound to ADP
3YGS 2.5 Å, Apaf-1 card in complex with prodomain of procaspase-9
8XQK 2.85 Å, The Crystal Structure of Apaf from Biortus.
5WVC 2.99 Å, Structure of the CARD-CARD disk
3JBT 3.8 Å, Atomic structure of the Apaf-1 apoptosome
5JUY 4.1 Å, Active human apoptosome with procaspase-9
5WVE 4.4 Å, Apaf-1-Caspase-9 holoenzyme
3J2T 9.5 Å, An improved model of the human apoptosome
1C15 Solution structure of apaf-1 card

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