CCM2 HHD in complex with MEKK3 NPB1. Determined by X-ray diffraction at 2.35 Å resolution. Released 1 Jul 2015.
Explore 4Y5O in 3D Show helices and sheets RCSB PDB PDBe
4Y5O contains 14 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 296-309 | 14 | |
| α-helix | 312-326 | 15 | |
| α-helix | 331-341 | 11 | |
| α-helix | 344-346 | 3 | |
| α-helix | 347-353 | 7 | |
| α-helix | 354-356 | 3 | |
| α-helix | 359-367 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1-14 | 14 | |
| α-helix | 44 | 1 | |
| β-strand | 45-51 | 7 | 1 |
| β-strand | 54-60 | 7 | 1 |
| α-helix | 61 | 1 | |
| α-helix | 64-65 | 2 | |
| α-helix | 66-77 | 12 | |
| β-strand | 82-85 | 4 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-93 | 2 | 1 |
| α-helix | 97-109 | 13 | |
| β-strand | 116-121 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Malcavernin | A | protein | 98 | Homo sapiens | Q9BSQ5 (AlphaFold model) |
| Mitogen-activated protein kinase kinase kinase 3 | B | protein | 126 | Homo sapiens | Q99759 (AlphaFold model) |
>4Y5O_1 Malcavernin (chains A) GSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQL YGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRG
>4Y5O_2 Mitogen-activated protein kinase kinase kinase 3 (chains B) GSMDEQEALNSIMNDLVALQMNRRHRMPGYETMKNKDTGHSNRQSDVRIKFEHNGERRII AFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDLDKAIDILDRSSSMKSLRI LLLSQD
Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex. Fisher, O.S., Deng, H., Liu, D. et al. Nat Commun (2015) 6:7937-7937. DOI 10.1038/ncomms8937 · PubMed
Other PDB entries of the same protein (UniProt Q9BSQ5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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