Research workbench
Aldolase, rabbit muscle (beam-tilt refinement X4)
Analyse Aldolase, rabbit muscle (beam-tilt refinement X4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KA4
- 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 · 47% 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 | 47% helix, 16% strand | P00883 |
Pockets
15 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 523 | 0.83 | 0.89 | 68 | empty |
| 2 | 850 | 0.80 | 0.82 | 105 | empty |
| 3 | 287 | 0.77 | 0.89 | 42 | empty |
| 4 | 89 | 0.74 | 0.97 | 32 | empty |
| 5 | 370 | 0.73 | 0.84 | 51 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1286 Ų buried · 27 hydrogen bonds · protein-protein
- A–C · 1233 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 1152 Ų buried · 13 hydrogen bonds · protein-protein
- B–A · 1148 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 27 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 7KA4 · PDBe 7KA4 · UniProt P00883
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