5WVC: CARD-CARD disk

Structure of the CARD-CARD disk. Determined by X-ray diffraction at 2.99 Å resolution. Released 19 Apr 2017.

Method: X-ray diffraction
Resolution: 2.99 Å
Organism: Homo sapiens
Chains: 6
Atoms: 4,796
Mol. weight: 86.4 kDa
Released: 19 Apr 2017

Explore 5WVC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5WVC contains 49 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: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	3-11	9
α-helix	13-17	5
α-helix	22-32	11
α-helix	37-44	8
α-helix	49-60	12
α-helix	65-77	13
α-helix	81-88	8
α-helix	91-94	4

Chain B: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	200-202	3
α-helix	203-211	9
α-helix	213-219	7
α-helix	225-231	7
α-helix	237-245	9
α-helix	251-261	11
α-helix	262-264	3
α-helix	269-279	11
α-helix	283-297	15

Chain C: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	3-11	9
α-helix	13-19	7
α-helix	22-32	11
α-helix	37-44	8
α-helix	49-61	13
α-helix	65-77	13
α-helix	81-88	8
α-helix	91-93	3

Chain D: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	200-202	3
α-helix	203-211	9
α-helix	213-219	7
α-helix	225-231	7
α-helix	237-244	8
α-helix	251-261	11
α-helix	262-264	3
α-helix	269-279	11
α-helix	283-299	17

Chain E: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	3-11	9
α-helix	13-19	7
α-helix	22-32	11
α-helix	37-44	8
α-helix	49-62	14
α-helix	65-77	13
α-helix	81-88	8

Chain F: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	203-211	9
α-helix	213-219	7
α-helix	225-231	7
α-helix	237-244	8
α-helix	251-261	11
α-helix	262-264	3
α-helix	269-278	10
α-helix	283-299	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Apoptotic protease-activating factor 1	A, C, E	protein	95	Homo sapiens	O14727 (AlphaFold model)
Caspase	B, D, F	protein	151	Homo sapiens	P55211 (AlphaFold model)

Sequence of entity 1 (A, C, E), FASTA

>5WVC_1 Apoptotic protease-activating factor 1 (chains A, C, E)
MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMI
LKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVS

Sequence of entity 2 (B, D, F), FASTA

>5WVC_2 Caspase (chains B, D, F)
MGSSHHHHHHSSGLVPRGSHMASMDEADRRLLRRCRLRLVEELQVDQLWDVLLSRELFRP
HMIEDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFLRTNRQAAK
LSKPTLENLTPVVLRPEIRKPEVLRPETPRP

Primary citation

Structural Insights into DD-Fold Assembly and Caspase-9 Activation by the Apaf-1 Apoptosome. Su, T.W., Yang, C.Y., Kao, W.P. et al. Structure (2017) 25:407-420. DOI 10.1016/j.str.2016.12.019 · 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
4RHW 2.1 Å, Crystal structure of Apaf-1 CARD and caspase-9 CARD complex
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.
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

Browse structure collections

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