MolNFT v1 · #145599 · protein
The structure of the CEP63-CEP152 heterotetrameric complex
6CSU: “The structure of the CEP63-CEP152 heterotetrameric complex”. X-ray diffraction. MolNFT v1 #145599 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6CSU
- Type
- protein
- Length
- 179 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O94986, Q96MT8
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 51 | — | O94986 |
| C | — | protein | 43 | — | Q96MT8 |
| D | — | protein | 52 | — | O94986 |
| A | — | protein | 33 | — | Q96MT8 |
Compared structures
- 6CSU · The structure of the Cep63-Cep152 heterotetrameric complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q96MT8 · AlphaFold monomer V2.0 prediction for centrosomal protein of 63 kda (Q96MT8) · a predicted model of the same protein · chain A against A, TM-score 0.91
- O94986 · AlphaFold monomer V2.0 prediction for centrosomal protein of 152 kda (O94986) · a predicted model of the same protein · chain D against A, TM-score 0.91
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 O94986
- Every structure of UniProt Q96MT8
- Elsewhere: RCSB PDB 6CSU · PDBe 6CSU · UniProt O94986 · UniProt Q96MT8
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