MolNFT v1 · #135904 · protein
Cryo-EM MAP of protofilament of microtubule doublet
5UCY: “Cryo-EM MAP of protofilament of microtubule doublet”. Electron microscopy, 3 ligands (GTP, GDP, MG). MolNFT v1 #135904 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UCY
- Type
- protein
- Length
- 870 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P41351, P41352
- Ligands
- GTP, GDP, MG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 441 | — | P41351 |
| B | — | protein | 429 | — | P41352 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · chains A, B
- GDP · Guanosine-5'-diphosphate · ligand · chains B
- MG · Magnesium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UCY · Cryo-EM map of protofilament of microtubule doublet · the same entry in another collection · chain B against B, TM-score 1.00
- P41352 · AlphaFold monomer V2.0 prediction for tubulin beta chain (P41352) · a predicted model of the same protein · chain B against A, TM-score 0.98
- P41351 · AlphaFold monomer V2.0 prediction for tubulin alpha chain (P41351) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P41351
- Every structure of UniProt P41352
- Elsewhere: RCSB PDB 5UCY · PDBe 5UCY · UniProt P41351 · UniProt P41352
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.