Research workbench
Crystal structure of hypothetical protein PH1109 from pyrococcus horikoshii
Analyse Crystal structure of hypothetical protein PH1109 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
- 2E6U
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein PH1109
- UniProt
- O58836
- Ligands
- COA, CA, CL
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Hypothetical protein PH1109 | protein | 142 | 39% helix, 19% strand | O58836 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains X
- CA · Calcium ion · metal · chains X
- CL · Chloride ion · ion · 3 copies · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.36 | 0.74 | 28 | COA |
Compared structures
- 2E6U · Crystal structure of hypothetical protein PH1109 from Pyrococcus horikoshii · the same entry in another collection · chain X against X, 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 O58836
- Elsewhere: RCSB PDB 2E6U · PDBe 2E6U · UniProt O58836
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