Research workbench
Cryo-EM structure of the CBF3-CEN3 complex of the budding yeast kinetochore
Analyse Cryo-EM structure of the CBF3-CEN3 complex of the budding yeast kinetochore in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GYS
- Type
- protein + DNA
- Length
- 4,545 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P35203, P40969, P52286, P32504
- Ligands
- ZN
Structure
electron microscopy · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, H | — | protein | 421 | — | P35203 |
| B, I | — | protein | 579 | — | P40969 |
| C | — | protein | 573 | — | P40969 |
| D, K | — | protein | 151 | — | P52286 |
| E, L | — | protein | 506 | — | P32504 |
| F | — | dna | 52 | — | — |
| G | — | dna | 52 | — | — |
| J | — | protein | 554 | — | P40969 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains B, C, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GYS · Cryo-EM structure of the CBF3-CEN3 complex of the budding yeast kinetochore · the same entry in another collection · chain L against L, TM-score 1.00
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 P35203
- Every structure of UniProt P40969
- Every structure of UniProt P52286
- Every structure of UniProt P32504
- Elsewhere: RCSB PDB 6GYS · PDBe 6GYS · UniProt P35203 · UniProt P40969 · UniProt P52286 · UniProt P32504
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.