1I4O: Xiap/caspase-7 complex

Crystal structure of the xiap/caspase-7 complex. Determined by X-ray diffraction at 2.4 Å resolution. Released 21 Mar 2001.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,124
Mol. weight: 96.27 kDa
Released: 21 Mar 2001

Explore 1I4O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I4O contains 21 α-helices and 36 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: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	59	1	1
α-helix	60-61	2
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	116-126	11
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	159-164	6
α-helix	172-174	3
β-strand	179-184	6	2
β-strand	190	1	4
β-strand	192	1	5
β-strand	213	1	6
β-strand	219-223	5	2
β-strand	229	1	4
β-strand	233-234	2	7
β-strand	238-239	2	7
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 B: 9 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	59	1	8
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	9
β-strand	149-151	3	9
β-strand	156-158	3	9
α-helix	159-163	5
α-helix	164-166	3
α-helix	172-174	3
β-strand	179-184	6	2
β-strand	190	1	10
β-strand	192	1	11
β-strand	195	1	6
β-strand	219-223	5	2
β-strand	229	1	10
β-strand	233-234	2	12
β-strand	238-239	2	12
α-helix	240-252	13
α-helix	258-272	15
β-strand	286	1	11
β-strand	290-293	4	2
β-strand	298	1	8

Chains C and D: 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	A, B	protein	280	Homo sapiens	P55210 (AlphaFold model)
Baculoviral iap repeat-containing protein 4	C, D	protein	141	Homo sapiens	P98170 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1I4O_1 CASPASE-7 (chains A, B)
AKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTG
MGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLS
HGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPIN
DTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILT
RVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ

Sequence of entity 2 (C, D), FASTA

>1I4O_2 BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 4 (chains C, D)
YLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHL
TPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRS
ESDAVSSDRNFPNSTNLPRNP

Primary citation

Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Huang, Y., Park, Y.C., Rich, R.L. et al. Cell (2001) 104:781-790. 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
2QL7 2.4 Å, Crystal Structure of Caspase-7 with inhibitor AC-IEPD-CHO

Browse structure collections

About this viewer

MolViewer shows 1I4O directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.