Research workbench
Cryo-EM structure of TSA201 cell ALPHA1B and betai and betaivb microtubules
Analyse Cryo-EM structure of TSA201 cell ALPHA1B and betai and betaivb microtubules in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N5N
- Type
- protein
- Length
- 5,124 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P07437, P68363
- Ligands
- G2P, GTP, MG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D, E, F | — | protein | 426 | — | P07437 |
| K, G, H, I, J, L | — | protein | 428 | — | P68363 |
Ligands and binding sites
- G2P · Phosphomethylphosphonic acid guanylate ester · ligand · 6 copies · chains B, G, A, C, H, D, L, E, F
- GTP · Guanosine-5'-triphosphate · ligand · 6 copies · chains B, K, G, A, H, C, I, D, J, E, L, F
- MG · Magnesium ion · metal · 12 copies · chains B, K, G, H, I, J, L, A, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5N5N · Cryo-EM structure of tsA201 cell alpha1B and betaI and betaIVb microtubules · the same entry in another collection · chain F against F, 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 P07437
- Every structure of UniProt P68363
- Elsewhere: RCSB PDB 5N5N · PDBe 5N5N · UniProt P07437 · UniProt P68363
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