Research workbench
The structure of the CEP63-CEP152 heterotetrameric complex
Analyse The structure of the CEP63-CEP152 heterotetrameric complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CSV
- Type
- protein
- Length
- 351 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Centrosomal protein of 63 KDA,CENTROSOMAL protein of 152 kda
- UniProt
- Q96MT8, O94986
Structure
x-ray diffraction · 4 distinct chains · 93% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Centrosomal protein of 63 KDA,CENTROSOMAL protein of 152 kda | protein | 90 | 91% helix, 0% strand | Q96MT8, O94986 |
| B | Centrosomal protein of 63 KDA,CENTROSOMAL protein of 152 kda | protein | 87 | 95% helix, 0% strand | Q96MT8, O94986 |
| C | Centrosomal protein of 63 KDA,CENTROSOMAL protein of 152 kda | protein | 88 | 92% helix, 0% strand | Q96MT8, O94986 |
| D | Centrosomal protein of 63 KDA,CENTROSOMAL protein of 152 kda | protein | 86 | 92% helix, 0% strand | Q96MT8, O94986 |
Interfaces
2 interfaces between chains.
- A–C · 2082 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 2051 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6CSV · The structure of the Cep63-Cep152 heterotetrameric complex · the same entry in another collection · chain A against A, TM-score 1.00
- O94986 · AlphaFold monomer V2.0 prediction for centrosomal protein of 152 kda (O94986) · a predicted model of the same protein · chain B against A, TM-score 0.59
- Q96MT8 · AlphaFold monomer V2.0 prediction for centrosomal protein of 63 kda (Q96MT8) · a predicted model of the same protein · chain D against A, TM-score 0.52
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q96MT8
- Every structure of UniProt O94986
- Elsewhere: RCSB PDB 6CSV · PDBe 6CSV · UniProt Q96MT8 · UniProt O94986
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