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Crystal structure of frv operon protein frvx (PH1821)FROM pyrococcus horikoshii OT3
Analyse Crystal structure of frv operon protein frvx (PH1821)FROM pyrococcus horikoshii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PE3
- Type
- protein
- Length
- 1,318 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 354AA long hypothetical operon protein frv
- UniProt
- O59485
- Pockets
- 15 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 354AA long hypothetical operon protein frv | protein | 330 | 28% helix, 28% strand | O59485 |
| B, C | 354AA long hypothetical operon protein frv | protein | 328 | 29% helix, 29% strand | O59485 |
| D | 354AA long hypothetical operon protein frv | protein | 332 | 28% helix, 28% strand | O59485 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.74 | 0.86 | 35 | empty |
| 2 | 65 | 0.71 | 0.97 | 23 | empty |
| 3 | 400 | 0.61 | 0.76 | 39 | empty |
| 4 | 287 | 0.56 | 0.77 | 39 | empty |
| 5 | 301 | 0.56 | 0.76 | 38 | empty |
Interfaces
4 interfaces between chains.
- A–D · 1855 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 1186 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 1171 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 1159 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2PE3 · Crystal structure of Frv operon protein FRVX (PH1821)from pyrococcus horikoshii OT3 · the same entry in another collection · chain A against A, TM-score 1.00
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 O59485
- Elsewhere: RCSB PDB 2PE3 · PDBe 2PE3 · UniProt O59485
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