4TVQ: CCM3

CCM3 in complex with CCM2 LD-like motif. Determined by X-ray diffraction at 2.8 Å resolution. Released 25 Mar 2015.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 5
Atoms: 5,969
Mol. weight: 101.45 kDa
Released: 25 Mar 2015

Explore 4TVQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4TVQ contains 51 α-helices and 0 β-strands across 5 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: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	20-21	2
α-helix	22-26	5
α-helix	27-31	5
α-helix	39-54	16
α-helix	58-68	11
α-helix	70-83	14
α-helix	109-115	7
α-helix	117-120	4
α-helix	124-132	9
α-helix	167-184	18
α-helix	187-206	20

Chain B: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	17-19	3
α-helix	20-21	2
α-helix	22-26	5
α-helix	27-36	10
α-helix	38-54	17
α-helix	58-68	11
α-helix	70-83	14
α-helix	84-86	3
α-helix	98-114	17
α-helix	117-120	4
α-helix	124-148	25
α-helix	162-183	22
α-helix	187-208	22

Chain C: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	5-12	8
α-helix	17-19	3
α-helix	20-21	2
α-helix	22-26	5
α-helix	27-36	10
α-helix	38-54	17
α-helix	58-68	11
α-helix	70-83	14
α-helix	98-114	17
α-helix	117-119	3
α-helix	124-148	25
α-helix	159-184	26
α-helix	187-209	23

Chain D: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	17-19	3
α-helix	20-21	2
α-helix	22-26	5
α-helix	27-33	7
α-helix	38-54	17
α-helix	58-67	10
α-helix	70-82	13
α-helix	83-85	3
α-helix	98-115	18
α-helix	117-120	4
α-helix	124-148	25
α-helix	159-184	26
α-helix	187-209	23

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	225-238	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cerebral cavernous malformations 3 protein	A, B, C, D	protein	214	Homo sapiens	Q9BUL8 (AlphaFold model)
Cerebral cavernous malformations 2 protein	E	protein	16	Homo sapiens	Q9BSQ5 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4TVQ_1 Cerebral cavernous malformations 3 protein (chains A, B, C, D)
GHMRMTMEEMKNEAETTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGL
TQDIIMKILEKKSVEVNFTESLLRMAADDVEEYMIERPEPEFQDLNEKARALKQILSKIP
DEINDRVRFLQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTL
KTYFKDGKAINVFVSANRLIHQTNLILQTFKTVA

Sequence of entity 2 (E), FASTA

>4TVQ_2 Cerebral cavernous malformations 2 protein (chains E)
STIDFLDRAIFDGAST

Primary citation

CCM2-CCM3 interaction stabilizes their protein expression and permits endothelial network formation. Draheim, K.M., Li, X., Zhang, R. et al. J Cell Biol (2015) 208:987-1001. DOI 10.1083/jcb.201407129 · PubMed

Other PDB entries of the same protein (UniProt Q9BUL8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4GEH 1.95 Å, Crystal structure of MST4 dimerization domain complex with PDCD10
3AJM 2.3 Å, Crystal structure of programmed cell death 10 in complex with inositol…
3W8I 2.4 Å, Crystal structure of CCM3 in complex with the C-terminal regulatory domain of MST4
3W8H 2.43 Å, Crystal structure of CCM3 in complex with the C-terminal regulatory domain of STK25
3L8I 2.5 Å, Crystal structure of CCM3, a cerebral cavernous malformation protein critical for…
3RQG 2.5 Å, Cerebral cavernous malformation 3 (CCM3) in complex with paxillin LD4
3RQF 2.7 Å, Cerebral cavernous malformation 3 (CCM3) in complex with paxillin LD2
3RQE 2.8 Å, Cerebral cavernous malformation 3 (CCM3) in complex with paxillin LD1
3L8J 3.05 Å, Crystal structure of CCM3, a cerebral cavernous malformation protein critical for…

Browse structure collections

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