Research workbench
Crystal structure of the L88A mutant of hslv from escherichia COLI
Analyse Crystal structure of the L88A mutant of hslv from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G4E
- Type
- protein
- Length
- 2,028 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent protease subunit hslv
- EC
- 3.4.25.2
- UniProt
- P0A7B8
- Pockets
- 12 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | ATP-dependent protease subunit hslv (EC 3.4.25.2) | protein | 169 | 36% helix, 31% strand | P0A7B8 |
Pockets
12 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 971 | 0.79 | 0.81 | 128 | empty |
| 2 | 1125 | 0.79 | 0.80 | 130 | empty |
| 3 | 1096 | 0.78 | 0.80 | 127 | empty |
| 4 | 844 | 0.73 | 0.78 | 94 | empty |
| 5 | 813 | 0.73 | 0.78 | 93 | empty |
Interfaces
24 interfaces between chains.
- B–H · 679 Ų buried · 3 hydrogen bonds · protein-protein
- D–F · 677 Ų buried · 6 hydrogen bonds · protein-protein
- C–E · 676 Ų buried · 6 hydrogen bonds · protein-protein
- J–K · 671 Ų buried · 3 hydrogen bonds · protein-protein
- A–G · 666 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- P0A7B8 · AlphaFold monomer V2.0 prediction for ATP-dependent protease subunit hslv (P0A7B8) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P0A7B8
- Elsewhere: RCSB PDB 4G4E · PDBe 4G4E · UniProt P0A7B8
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