Research workbench
Phage TP901-1 baseplate tripod
Analyse Phage TP901-1 baseplate tripod in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U6X
- Type
- protein
- Length
- 3,564 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bpp; ORF48
- UniProt
- Q9G096, Q9AZ56
- Ligands
- BR
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R | Bpp | protein | 163 | 10% helix, 39% strand | Q9G096 |
| S, T, U, X, Y, Z | ORF48 | protein | 105 | 3% helix, 49% strand | Q9AZ56 |
Ligands and binding sites
- BR · Bromide ion · ion · 18 copies · chains D, E, F, C, G, H, I, A, K, O, N, R, M, P, Q, L, S, T, U, X, Y, Z
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 598 | 0.78 | 0.84 | 72 | empty |
| 2 | 702 | 0.78 | 0.83 | 83 | empty |
| 3 | 668 | 0.78 | 0.83 | 79 | empty |
| 4 | 739 | 0.78 | 0.82 | 85 | empty |
| 5 | 608 | 0.77 | 0.83 | 68 | empty |
Interfaces
68 interfaces between chains.
- K–L · 2517 Ų buried · 49 hydrogen bonds · protein-protein
- Q–R · 2511 Ų buried · 46 hydrogen bonds · protein-protein
- A–C · 2495 Ų buried · 47 hydrogen bonds · protein-protein
- H–I · 2495 Ų buried · 54 hydrogen bonds · protein-protein
- N–O · 2490 Ų buried · 49 hydrogen bonds · protein-protein
Compared structures
- 3U6X · Phage TP901-1 baseplate tripod · 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 Q9G096
- Every structure of UniProt Q9AZ56
- Elsewhere: RCSB PDB 3U6X · PDBe 3U6X · UniProt Q9G096 · UniProt Q9AZ56
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