6CL2: Caspase-7

Caspase-7 in complex with Ac-ATS009-KE. Determined by X-ray diffraction at 2.35 Å resolution. Released 6 Mar 2019.

Method: X-ray diffraction
Resolution: 2.35 Å
Organisms: Homo sapiens, synthetic construct
Chains: 6
Atoms: 3,829
Mol. weight: 72.73 kDa
Released: 6 Mar 2019

Explore 6CL2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CL2 contains 19 α-helices and 40 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: 7 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	59	1	1
β-strand	66-74	9	2
α-helix	80-82	3
α-helix	84-86	3
α-helix	90-104	15
β-strand	106-112	7	2
α-helix	116-128	13
β-strand	134-142	9	2
β-strand	145-146	2	3
β-strand	149-152	4	3
β-strand	155-158	4	3
α-helix	159-164	6
α-helix	168-170	3
α-helix	172-174	3
β-strand	179-184	6	2
β-strand	190	1	4
β-strand	192	1	5
β-strand	195	1	6

Chains B and D: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	213	1	7
β-strand	219-223	5	2
β-strand	229	1	4
β-strand	232-234	3	8
β-strand	238-239	2	8
α-helix	240-252	13
α-helix	258-272	15
α-helix	280-282	3
β-strand	286	1	5
β-strand	290-293	4	2
β-strand	298	1	1

Chain C: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	59	1	9
β-strand	66-74	9	2
α-helix	80-82	3
α-helix	84-86	3
α-helix	90-104	15
β-strand	107-112	6	2
α-helix	116-128	13
β-strand	134-142	9	2
β-strand	145-146	2	10
β-strand	149-152	4	10
β-strand	155-158	4	10
α-helix	159-164	6
α-helix	172-174	3
β-strand	179-184	6	2
β-strand	190	1	11
β-strand	192	1	12
β-strand	195	1	7

Chains E and F: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	404-405	2	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Caspase-7 subunit p20	A, C	protein	198	Homo sapiens	P55210 (AlphaFold model)
Caspase-7 subunit p11	B, D	protein	113	Homo sapiens	P55210 (AlphaFold model)
Ace-1MH-asp-PF5-phe-1U8	E, F	protein	6	synthetic construct

Sequence of entity 1 (A, C), FASTA

>6CL2_1 Caspase-7 subunit p20 (chains A, C)
MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQY
NMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQ
DLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKL
FFIQACRGTELDDGIQAD

Sequence of entity 2 (B, D), FASTA

>6CL2_2 Caspase-7 subunit p11 (chains B, D)
SGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEI
MQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQLEHHHHHH

Sequence of entity 3 (E, F), FASTA

>6CL2_3 ACE-1MH-ASP-PF5-PHE-1U8 (chains E, F)
XXDFFX

Primary citation

Selective and Rapid Cell-Permeable Inhibitor of Human Caspase-3. Solania, A., Gonzalez-Paez, G.E., Wolan, D.W. ACS Chem Biol (2019) 14:2463-2470. DOI 10.1021/acschembio.9b00564 · PubMed

Other PDB entries of the same protein (UniProt P55210 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4JR2 1.65 Å, Human procaspase-7/caspase-7 heterodimer bound to Ac-DEVD-CMK
4JB8 1.7 Å, Caspase-7 in Complex with DARPin C7_16
2QL9 2.14 Å, Crystal Structure of Caspase-7 with inhibitor AC-DQMD-CHO
4JR1 2.15 Å, Human procaspase-7 bound to Ac-DEVD-CMK
5K20 2.2 Å, Caspase-7 S239E Phosphomimetic
2QLB 2.25 Å, Crystal Structure of caspase-7 with inhibitor AC-ESMD-CHO
4LSZ 2.26 Å, Caspase-7 in Complex with DARPin D7.18
4ZVR 2.3 Å, Caspase-7 Variant 4 (V4) with reprogrammed substrate specificity due to…
2QL5 2.34 Å, Crystal Structure of caspase-7 with inhibitor AC-DMQD-CHO
1F1J 2.35 Å, Crystal structure of caspase-7 in complex with acetyl-asp-glu-val-asp-cho
1I4O 2.4 Å, Crystal structure of the xiap/caspase-7 complex
2QL7 2.4 Å, Crystal Structure of Caspase-7 with inhibitor AC-IEPD-CHO

Browse structure collections

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