Research workbench
Crystal structure of BT1762-1763
Analyse Crystal structure of BT1762-1763 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T3R
- Type
- protein
- Length
- 1,359 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Susd homolog; Susc homolog
- UniProt
- Q8A6W4, Q8A6W3
- Ligands
- MG, NA
- Pockets
- 18 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Susd homolog | protein | 553 | 43% helix, 9% strand | Q8A6W4 |
| D | Susc homolog | protein | 806 | 8% helix, 46% strand | Q8A6W3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.82 | 0.95 | 37 | empty |
| 2 | 932 | 0.74 | 0.78 | 98 | empty |
| 3 | 473 | 0.68 | 0.79 | 55 | empty |
| 4 | 254 | 0.58 | 0.79 | 34 | empty |
| 5 | 188 | 0.57 | 0.81 | 24 | empty |
Interfaces
1 interface between chains.
- A–D · 4323 Ų buried · 63 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5T3R · Crystal structure of BT1762-1763 · 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 Q8A6W4
- Every structure of UniProt Q8A6W3
- Elsewhere: RCSB PDB 5T3R · PDBe 5T3R · UniProt Q8A6W4 · UniProt Q8A6W3
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