3C3O: ALIX Bro1-domain:CHMIP4A co-crystal structure

ALIX Bro1-domain:CHMIP4A co-crystal structure. Determined by X-ray diffraction at 2.15 Å resolution. Released 10 Jun 2008.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,043
Mol. weight: 44.35 kDa
Released: 10 Jun 2008

Explore 3C3O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3C3O contains 17 α-helices and 3 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, 3 β-strands

Element	Residues	Length	Sheet
α-helix	8-11	4
β-strand	12	1	1
α-helix	18-22	5
α-helix	42-55	14
α-helix	57-58	2
α-helix	62-76	15
β-strand	93-96	4	1
β-strand	110-113	4	1
α-helix	116-135	20
α-helix	143-171	29
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

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	212-218	7

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 4a peptide	B	protein	13		Q9BY43 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3C3O_1 Programmed cell death 6-interacting protein (chains A)
MHHHHHHHHHHSGQNLYFQGHMATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQY
CRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAF
DKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGA
FLHIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQ
AADYFGDAFKQCQYKDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQH
AAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVK
STPVNVPISQKFTDLFEKMV

Sequence of entity 2 (B), FASTA

>3C3O_2 Charged multivesicular body protein 4a peptide (chains B)
DEEALKQLAEWVS

Primary citation

ALIX-CHMP4 interactions in the human ESCRT pathway. McCullough, J., Fisher, R.D., Whitby, F.G. et al. Proc Natl Acad Sci U S A (2008) 105:7687-7691. DOI 10.1073/pnas.0801567105 · 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
5V3R 1.91 Å, CHMP4C 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
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

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