Research workbench
Structure of PH1811 protein from pyrococcus horikoshii
Analyse Structure of PH1811 protein 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
- 2EKN
- Type
- protein
- Length
- 435 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable molybdenum cofactor biosynthesis protein C
- UniProt
- O59475
- Pockets
- 4 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable molybdenum cofactor biosynthesis protein C | protein | 145 | 35% helix, 33% strand | O59475 |
| B, C | Probable molybdenum cofactor biosynthesis protein C | protein | 145 | 35% helix, 32% strand | O59475 |
Ligands and binding sites
- FLC · Citrate anion · additive · 2 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.53 | 0.80 | 34 | FLC |
| 2 | 107 | 0.48 | 0.80 | 22 | empty |
| 3 | 191 | 0.45 | 0.74 | 23 | empty |
| 4 | 119 | 0.44 | 0.77 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1845 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 723 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 236 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2EKN · Structure of PH1811 protein from Pyrococcus horikoshii · the same entry in another collection · chain A against A, TM-score 1.00
- O59475 · AlphaFold monomer V2.0 prediction for probable cyclic pyranopterin monophosphate synthase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O59475
- Elsewhere: RCSB PDB 2EKN · PDBe 2EKN · UniProt O59475
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