MolNFT v2 · #168310 · protein
Rabbit muscle aldolase determined using single-particle cryo-EM at 200 keV
6V20: “Rabbit muscle aldolase determined using single-particle cryo-EM at 200 keV”. Electron microscopy at 2.13. MolNFT v2 #168310 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6V20
- Type
- protein
- Length
- 1,372 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.13
- Source
- Oryctolagus cuniculus
- UniProt
- P00883
Structure
electron microscopy · resolution 2.13 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 343 | — | P00883 |
Compared structures
- 6V20 · Rabbit muscle aldolase determined using single-particle cryo-EM at 200 kev · the same entry in another collection · chain D against D, TM-score 1.00
- P00883 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase a (P00883) · a predicted model of the same protein · chain C against A, 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 P00883
- Elsewhere: RCSB PDB 6V20 · PDBe 6V20 · UniProt P00883
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