Research workbench
Structure of B.SUBTILIS lrpc
Analyse Structure of B.SUBTILIS lrpc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CFX
- Type
- protein
- Length
- 1,120 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional regulator lrpc
- UniProt
- P96582
- Pockets
- 11 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Hth-type transcriptional regulator lrpc | protein | 140 | 42% helix, 31% strand | P96582 |
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1059 | 0.72 | 0.76 | 81 | empty |
| 2 | 1032 | 0.72 | 0.76 | 69 | empty |
| 3 | 1036 | 0.71 | 0.75 | 79 | empty |
| 4 | 967 | 0.71 | 0.75 | 67 | empty |
| 5 | 539 | 0.71 | 0.80 | 105 | empty |
Interfaces
16 interfaces between chains.
- D–G · 2623 Ų buried · 44 hydrogen bonds · protein-protein
- C–H · 2615 Ų buried · 41 hydrogen bonds · protein-protein
- E–F · 2594 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 2547 Ų buried · 39 hydrogen bonds · protein-protein
- A–H · 434 Ų buried · 3 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 P96582
- Elsewhere: RCSB PDB 2CFX · PDBe 2CFX · UniProt P96582
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