Research workbench
Structure of the protease production regulatory protein hpr from bacillus subtilis.
Analyse Structure of the protease production regulatory protein hpr from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FXA
- Type
- protein
- Length
- 652 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease production regulatory protein hpr
- UniProt
- P11065
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 70% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease production regulatory protein hpr | protein | 156 | 71% helix, 6% strand | P11065 |
| B | Protease production regulatory protein hpr | protein | 180 | 68% helix, 10% strand | P11065 |
| C | Protease production regulatory protein hpr | protein | 160 | 72% helix, 6% strand | P11065 |
| D | Protease production regulatory protein hpr | protein | 156 | 71% helix, 6% strand | P11065 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 14 copies · chains A, B, C, D
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A, B, C, D
- P6G · Hexaethylene glycol · additive · chains A, B
- PGE · Triethylene glycol · additive · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1032 | 0.83 | 0.84 | 111 | EDO, PGE |
| 2 | 170 | 0.73 | 0.90 | 27 | P6G |
| 3 | 163 | 0.72 | 0.90 | 27 | 1PE |
| 4 | 359 | 0.70 | 0.83 | 52 | 1PE |
| 5 | 85 | 0.32 | 0.73 | 16 | empty |
Interfaces
6 interfaces between chains.
- A–B · 3429 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 3139 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 297 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 267 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 168 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 2FXA · Structure of the Protease Production Regulatory Protein hpr from Bacillus subtilis. · the same entry in another collection · chain D against D, TM-score 1.00
- P11065 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator hpr (P11065) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P11065
- Elsewhere: RCSB PDB 2FXA · PDBe 2FXA · UniProt P11065
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