3L8I: Programmed cell death protein 10

Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 May 2010.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,725
Mol. weight: 99.72 kDa
Released: 19 May 2010

Explore 3L8I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3L8I contains 54 α-helices and 0 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: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	20-21	2
α-helix	22-26	5
α-helix	27-31	5
α-helix	34-54	21
α-helix	58-67	10
α-helix	70-83	14
α-helix	98-115	18
α-helix	117-119	3
α-helix	124-148	25
α-helix	149-151	3
α-helix	158-184	27
α-helix	188-211	24

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	11-14	4
α-helix	17-19	3
α-helix	20-21	2
α-helix	22-26	5
α-helix	27-34	8
α-helix	38-54	17
α-helix	58-68	11
α-helix	70-83	14
α-helix	84-87	4
α-helix	98-114	17
α-helix	117-120	4
α-helix	124-151	28
α-helix	160-184	25
α-helix	187-207	21

Chain C: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	5-13	9
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	98-115	18
α-helix	117-119	3
α-helix	124-149	26
α-helix	159-184	26
α-helix	188-209	22

Chain D: 15 helices, 0 β-strands

Element	Residues	Length
α-helix	9-13	5
α-helix	15-16	2
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	86-88	3
α-helix	98-114	17
α-helix	117-120	4
α-helix	124-150	27
α-helix	159-184	26
α-helix	187-207	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Programmed cell death protein 10	A, B, C, D	protein	214	Homo sapiens	Q9BUL8 (AlphaFold model)

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

>3L8I_1 Programmed cell death protein 10 (chains A, B, C, D)
GHMRMTMEEMKNEAETTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGL
TQDIIMKILEKKSVEVNFTESLLRMAADDVEEYMIERPEPEFQDLNEKARALKQILSKIP
DEINDRVRFLQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTL
KTYFKDGKAINVFVSANRLIHQTNLILQTFKTVA

Primary citation

Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity. Li, X., Zhang, R., Zhang, H. et al. J Biol Chem (2010) 285:24099-24107. DOI 10.1074/jbc.M110.128470 · 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
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
4TVQ 2.8 Å, CCM3 in complex with CCM2 LD-like motif
3L8J 3.05 Å, Crystal structure of CCM3, a cerebral cavernous malformation protein critical for…

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