Research workbench
Engineered disulfide cross-linked closed conformation of the yeast gamma-TURC(SS)
Analyse Engineered disulfide cross-linked closed conformation of the yeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M2W
- Type
- protein
- Length
- 4,827 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53378, P38863, P53540, P32380
- Ligands
- GTP
Structure
electron microscopy · 9 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 441 | — | P53378 |
| A | — | protein | 453 | — | P53378 |
| C | — | protein | 445 | — | P53378 |
| D | — | protein | 447 | — | P53378 |
| E | — | protein | 707 | — | P38863 |
| F, H | — | protein | 674 | — | P53540 |
| G | — | protein | 712 | — | P38863 |
| U, X | — | protein | 42 | — | P32380 |
| K, Y | — | protein | 95 | — | P32380 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 4 copies · chains B, A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M2W · Engineered disulfide cross-linked closed conformation of the Yeast gamma-TuRC(SS) · the same entry in another collection · chain Y against Y, 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 P53378
- Every structure of UniProt P38863
- Every structure of UniProt P53540
- Every structure of UniProt P32380
- Elsewhere: RCSB PDB 7M2W · PDBe 7M2W · UniProt P53378 · UniProt P38863 · UniProt P53540 · UniProt P32380
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