7WR1: P32 of caspase-4 C258A mutant

P32 of caspase-4 C258A mutant in complex with OspC3 C-terminal ankyrin-repeat domain. Determined by X-ray diffraction at 2.13 Å resolution. Released 25 Jan 2023.

Method: X-ray diffraction
Resolution: 2.13 Å
Organisms: Homo sapiens, Shigella flexneri
Chains: 4
Atoms: 6,593
Mol. weight: 100.92 kDa
Released: 25 Jan 2023

Explore 7WR1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7WR1 contains 50 α-helices and 24 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: 13 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	107-110	4
α-helix	111-120	10
β-strand	125	1	1
α-helix	131-133	3
β-strand	137-142	6	2
α-helix	155-168	14
β-strand	172-177	6	2
α-helix	181-192	12
α-helix	195-199	5
β-strand	203-210	8	2
β-strand	211	1	3
β-strand	215-217	3	3
β-strand	228-230	3	3
α-helix	231-237	7
α-helix	244-246	3
β-strand	251-258	8	2
α-helix	290-296	7
β-strand	300-305	6	2
α-helix	307-309	3
α-helix	321-333	13
α-helix	339-349	11
α-helix	356-358	3
β-strand	361-363	3	2
β-strand	370	1	1

Chain B: 13 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	107-110	4
α-helix	111-120	10
α-helix	122-124	3
β-strand	125	1	4
α-helix	131-133	3
β-strand	137-142	6	5
α-helix	155-168	14
β-strand	172-177	6	5
α-helix	181-192	12
α-helix	195-199	5
β-strand	203-210	8	5
β-strand	211	1	6
β-strand	215-217	3	6
β-strand	228-230	3	6
α-helix	231-237	7
α-helix	244-246	3
β-strand	251-258	8	5
α-helix	289-296	8
β-strand	300-305	6	5
α-helix	321-333	13
α-helix	339-348	10
α-helix	356-358	3
β-strand	361-363	3	5
β-strand	370	1	4

Chains C and D: 12 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	348-353	6
α-helix	357-363	7
α-helix	367-379	13
α-helix	383-392	10
α-helix	397-404	8
α-helix	410-414	5
α-helix	417-422	6
α-helix	425-427	3
α-helix	428-436	9
α-helix	444-446	3
α-helix	455-462	8
α-helix	465-473	9
β-strand	483	1	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Caspase-4	A, B	protein	280	Homo sapiens	P49662 (AlphaFold model)
OspC3	C, D	protein	161	Shigella flexneri	A0A0H2US87 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7WR1_1 Caspase-4 (chains A, B)
SGRPSTDALKLCPHEEFLRLCKERAEEIYPIKERNNRTRLALIICNTEFDHLPPRNGADF
DITGMKELLEGLDYSVDVEENLTARDMESALRAFATRPEHKSSDSTFLVLMSHGILEGIC
GTVHDEKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQAARGANRGELWVRDSPASLEV
ASSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCC
HLEEVFRKVQQSFETPRAKAQMPTIERLSMTRYFYLFPGN

Sequence of entity 2 (C, D), FASTA

>7WR1_2 OspC3 (chains C, D)
GPLGSGRPMLSTDNFKKIKLRDISLEDAIKASNYEEINNKVTDKKMAHQALAYSLGNKKA
DIALYLLSKFNFTKQDVAEMEKMKNNRYCNLYDVEYLLSKDGANYKVLEYFINNGLVDVN
KKFQKVNSGDTMLDNAMKSKDSKMIDFLLKNGAILGKRFEI

Primary citation

Structural mechanisms of calmodulin activation of Shigella effector OspC3 to ADP-riboxanate caspase-4/11 and block pyroptosis. Hou, Y., Zeng, H., Li, Z. et al. Nat Struct Mol Biol (2023) 30:261-272. DOI 10.1038/s41594-022-00888-3 · PubMed

Other PDB entries of the same protein (UniProt P49662 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7WR6 1.96 Å, Crystal structure of ADP-riboxanated caspase-4 in complex with Af1521
6NRY 2.18 Å, Crystal structure of human caspase-4
7WR4 2.75 Å, Crystal structure of OspC3-calmodulin-caspase-4 complex
7WR0 2.8 Å, P32 of caspase-4 C258A mutant
7WR5 3.1 Å, Crystal structure of OspC3-calmodulin-caspase-4 complex binding with 2'-aF-NAD+
8J6K 3.12 Å, Crystal structure of pro-interleukin-18 and caspase-4 complex
8SPB 3.2 Å, Caspase-4/Pro-IL-18 complex
23BD 3.4 Å, Caspase-4 p22/p10 and human GSDMD complex
23BB 3.6 Å, Caspase-4 p20/p10 and human GSDMD
6KMZ 3.61 Å, caspase-4 P22/P10 C258A in complex with human GSDMD-C domain

Browse structure collections

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