Research workbench
Rabbit muscle aldolase determined using single-particle cryo-EM at 200 kev
Analyse Rabbit muscle aldolase determined using single-particle cryo-EM at 200 kev in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V20
- Type
- protein
- Length
- 1,372 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructose-bisphosphate aldolase a
- EC
- 4.1.2.13
- UniProt
- P00883
- Pockets
- 14 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 343 | 46% helix, 15% strand | P00883 |
Pockets
14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1154 | 0.88 | 0.89 | 123 | empty |
| 2 | 494 | 0.82 | 0.88 | 57 | empty |
| 3 | 743 | 0.80 | 0.83 | 98 | empty |
| 4 | 175 | 0.67 | 0.87 | 46 | empty |
| 5 | 161 | 0.66 | 0.87 | 45 | empty |
Interfaces
6 interfaces between chains.
- A–C · 1273 Ų buried · 23 hydrogen bonds · protein-protein
- B–D · 1273 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1180 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1179 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 75 Ų buried · 0 hydrogen bonds · protein-protein
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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