Research workbench
Aldolase, rabbit muscle (beam-tilt refinement X2)
Analyse Aldolase, rabbit muscle (beam-tilt refinement X2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KA2
- 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
- 15 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D | Fructose-bisphosphate aldolase a (EC 4.1.2.13) | protein | 343 | 48% helix, 16% strand | P00883 |
Pockets
15 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 370 | 0.83 | 0.92 | 51 | empty |
| 2 | 876 | 0.80 | 0.82 | 98 | empty |
| 3 | 296 | 0.77 | 0.89 | 47 | empty |
| 4 | 287 | 0.76 | 0.89 | 44 | empty |
| 5 | 131 | 0.73 | 0.93 | 36 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1420 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 1255 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 1099 Ų buried · 13 hydrogen bonds · protein-protein
- B–A · 1080 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 24 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 7KA2 · PDBe 7KA2 · UniProt P00883
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