MolNFT v1 · #34327 · protein
Structure of PH1503 protein from pyrococcus horikoshii OT3
2DCL · Hypothetical UPF0166 protein PH1503: “Structure of PH1503 protein from pyrococcus horikoshii OT3”. X-ray diffraction, 1 ligand (AMP), 5 pockets (best druggability 0.68). MolNFT v1 #34327 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2DCL
- Type
- protein
- Length
- 294 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical UPF0166 protein PH1503
- UniProt
- O59172
- Ligands
- AMP
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 24% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical UPF0166 protein PH1503 | protein | 99 | 22% helix, 41% strand | O59172 |
| B | Hypothetical UPF0166 protein PH1503 | protein | 98 | 22% helix, 44% strand | O59172 |
| C | Hypothetical UPF0166 protein PH1503 | protein | 97 | 27% helix, 41% strand | O59172 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 3 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.68 | 0.84 | 34 | AMP |
| 2 | 279 | 0.66 | 0.82 | 36 | AMP |
| 3 | 217 | 0.56 | 0.79 | 32 | AMP |
| 4 | 56 | 0.34 | 0.78 | 12 | empty |
| 5 | 63 | 0.29 | 0.73 | 12 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1133 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1036 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 928 Ų buried · 17 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 O59172
- Elsewhere: RCSB PDB 2DCL · PDBe 2DCL · UniProt O59172
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