5V3R: CHMP4C

CHMP4C in complex with ALIX BRO1. Determined by X-ray diffraction at 1.91 Å resolution. Released 12 Sept 2018.

Method: X-ray diffraction
Resolution: 1.91 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,006
Mol. weight: 44.75 kDa
Released: 12 Sept 2018

Explore 5V3R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5V3R contains 17 α-helices and 5 β-strands across 2 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: 16 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	8-11	4
β-strand	12	1	1
α-helix	18-23	6
α-helix	37-54	18
α-helix	62-76	15
β-strand	93-96	4	1
β-strand	103	1	2
β-strand	107	1	2
β-strand	110-113	4	1
α-helix	116-136	21
α-helix	143-170	28
α-helix	174-176	3
α-helix	181-205	25
α-helix	210-230	21
α-helix	241-266	26
α-helix	270-290	21
α-helix	298-314	17
α-helix	315-319	5
α-helix	326-328	3
α-helix	330-332	3
α-helix	340-342	3

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	222-232	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Programmed cell death 6-interacting protein	A	protein	380	Homo sapiens	Q8WUM4 (AlphaFold model)
Charged multivesicular body protein 4c	B	protein	18	Homo sapiens	Q96CF2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5V3R_1 Programmed cell death 6-interacting protein (chains A)
GHHHHHHHHHHSGENLYFQGHMATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQY
CRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAF
DKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGA
FLHIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQ
AADYFGDAFKQCQYKDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQH
AAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVK
STPVNVPISQKFTDLFEKMV

Sequence of entity 2 (B), FASTA

>5V3R_2 Charged multivesicular body protein 4c (chains B)
QRAEEEDDDIKQLAAWAT

Primary citation

A cancer-associated polymorphism in ESCRT-III disrupts the abscission checkpoint and promotes genome instability. Sadler, J.B.A., Wenzel, D.M., Williams, L.K. et al. Proc Natl Acad Sci U S A (2018) 115:E8900-E8908. DOI 10.1073/pnas.1805504115 · PubMed

Other PDB entries of the same protein (UniProt Q8WUM4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5WA1 1.87 Å, CHMP4C A232T in complex with ALIX BRO1
3E1R 2.0 Å, Midbody targeting of the ESCRT machinery by a non-canonical coiled-coil in CEP55
3C3R 2.02 Å, ALIX BRO1 CHMP4C complex
3C3Q 2.1 Å, ALIX Bro1-domain:CHMIP4B co-crystal structure
3C3O 2.15 Å, ALIX Bro1-domain:CHMIP4A co-crystal structure
2ZNE 2.2 Å, Crystal structure of Zn2+-bound form of des3-23ALG-2 complexed with Alix ABS peptide
6KP3 2.2 Å, Structure of sendai virus Y3/ALIX-BRO1 domain complex
2XS1 2.3 Å, Crystal Structure of ALIX in complex with the SIVmac239 PYKEVTEDL Late Domain
2XS8 2.5 Å, Crystal Structure of ALIX in complex with the SIVagmTan-1 AYDPARKLL Late Domain
2OEW 2.55 Å, Structure of ALIX/AIP1 Bro1 Domain
2R05 2.55 Å, Crystal Structure of ALIX/AIP1 in complex with the HIV-1 YPLASL Late Domain
2OEX 2.58 Å, Structure of ALIX/AIP1 V Domain

Browse structure collections

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