3RQG: Cerebral cavernous malformation 3

Cerebral cavernous malformation 3 (CCM3) in complex with paxillin LD4. Determined by X-ray diffraction at 2.5 Å resolution. Released 1 Jun 2011.

Method: X-ray diffraction
Resolution: 2.5 Å
Organisms: Homo sapiens, Homo Sapiens
Chains: 5
Atoms: 6,755
Mol. weight: 101.16 kDa
Released: 1 Jun 2011

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

Secondary structure: helices and β-sheets

3RQG contains 55 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	20-21	2
α-helix	22-26	5
α-helix	27-31	5
α-helix	38-54	17
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	154-156	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	70-82	13
α-helix	83-87	5
α-helix	98-115	18
α-helix	117-120	4
α-helix	124-149	26
α-helix	160-184	25
α-helix	187-207	21

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	27-33	7
α-helix	38-54	17
α-helix	58-68	11
α-helix	70-84	15
α-helix	98-115	18
α-helix	117-119	3
α-helix	124-149	26
α-helix	160-184	25
α-helix	188-207	20

Chain D: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	10-13	4
α-helix	15-16	2
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	70-83	14
α-helix	98-114	17
α-helix	117-120	4
α-helix	124-150	27
α-helix	158-184	27
α-helix	187-209	23

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	264-272	9

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)
Paxillin LD4 peptide	E	protein	13	Homo Sapiens	P49023 (AlphaFold model)

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

>3RQG_1 Programmed cell death protein 10 (chains A, B, C, D)
GHMRMTMEEMKNEAETTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGL
TQDIIMKILEKKSVEVNFTESLLRMAADDVEEYMIERPEPEFQDLNEKARALKQILSKIP
DEINDRVRFLQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTL
KTYFKDGKAINVFVSANRLIHQTNLILQTFKTVA

Sequence of entity 2 (E), FASTA

>3RQG_2 Paxillin LD4 peptide (chains E)
ATRELDELMASLS

Primary citation

Molecular Recognition of Leucine-Aspartate Repeat (LD) Motifs by the Focal Adhesion Targeting Homology Domain of Cerebral Cavernous Malformation 3 (CCM3). Li, X., Ji, W., Zhang, R. et al. J Biol Chem (2011) 286:26138-26147. DOI 10.1074/jbc.M110.211250 · 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…
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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