1I51: Caspase-7

Crystal structure of caspase-7 complexed with xiap. Determined by X-ray diffraction at 2.45 Å resolution. Released 23 Feb 2002.

Method: X-ray diffraction
Resolution: 2.45 Å
Organism: Homo sapiens
Chains: 6
Atoms: 3,974
Mol. weight: 84.92 kDa
Released: 23 Feb 2002

Explore 1I51 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I51 contains 19 α-helices and 38 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: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	59	1	1
β-strand	66-74	9	2
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	3
β-strand	149-151	3	3
β-strand	156-158	3	3
α-helix	159-163	5
α-helix	164-166	3
α-helix	168-174	7
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	233-234	2	8
β-strand	238-239	2	8
α-helix	240-252	13
α-helix	258-271	14
α-helix	280-282	3
β-strand	286	1	5
β-strand	290-293	4	2
β-strand	298	1	1

Chain C: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	59	1	9
β-strand	66-74	9	2
α-helix	90-104	15
β-strand	107-112	6	2
α-helix	116-127	12
β-strand	134-142	9	2
β-strand	145-146	2	10
β-strand	149-151	3	10
β-strand	156-158	3	10
α-helix	159-163	5
α-helix	164-166	3
α-helix	168-174	7
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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	136-142	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Caspase-7 subunit P20	A, C	protein	148	Homo sapiens	P55210 (AlphaFold model)
Caspase-7 subunit P11	B, D	protein	105	Homo sapiens	P55210 (AlphaFold model)
X-linked inhibitor of apoptosis protein	E, F	protein	117	Homo sapiens	P98170 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1I51_1 CASPASE-7 SUBUNIT P20 (chains A, C)
TRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIV
YNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGAR
CKTLLEKPKLFFIQACRGTELDDGIQAD

Sequence of entity 2 (B, D), FASTA

>1I51_2 CASPASE-7 SUBUNIT P11 (chains B, D)
SGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEI
MQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ

Sequence of entity 3 (E, F), FASTA

>1I51_3 X-LINKED INHIBITOR OF APOPTOSIS PROTEIN (chains E, F)
RDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYCEEARLKSFQNWPDYAHLTPRE
LASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSE

Primary citation

Structural basis of caspase-7 inhibition by XIAP. Chai, J., Shiozaki, E., Srinivasula, S.M. et al. Cell (2001) 104:769-780. DOI 10.1016/S0092-8674(01)00272-0 · 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
6CL2 2.35 Å, Caspase-7 in complex with Ac-ATS009-KE
1I4O 2.4 Å, Crystal structure of the xiap/caspase-7 complex

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