MolNFT v1 · #134467 · protein
Crystal structure of BT1762-1763
5T4Y · Susd homolog: “Crystal structure of BT1762-1763”. X-ray diffraction, 1 ligand (MG), 20 pockets (best druggability 0.84). MolNFT v1 #134467 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5T4Y
- Type
- protein
- Length
- 2,719 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Susd homolog; Susc homolog
- UniProt
- Q8A6W4, Q8A6W3
- Ligands
- MG
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Susd homolog | protein | 552 | 44% helix, 7% strand | Q8A6W4 |
| D, C | Susc homolog | protein | 807 | 8% helix, 49% strand | Q8A6W3 |
| B | Susd homolog | protein | 553 | 43% helix, 8% strand | Q8A6W4 |
Ligands and binding sites
- MG · Magnesium ion · metal · 5 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 216 | 0.84 | 0.96 | 45 | empty |
| 2 | 209 | 0.82 | 0.96 | 43 | empty |
| 3 | 888 | 0.81 | 0.83 | 138 | empty |
| 4 | 1144 | 0.75 | 0.78 | 129 | empty |
| 5 | 872 | 0.75 | 0.79 | 81 | empty |
Interfaces
5 interfaces between chains.
- B–C · 4354 Ų buried · 77 hydrogen bonds · protein-protein
- A–D · 4268 Ų buried · 73 hydrogen bonds · protein-protein
- D–C · 2792 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 364 Ų buried · 2 hydrogen bonds · protein-protein
- D–B · 347 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5T4Y · 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 5T4Y · PDBe 5T4Y · UniProt Q8A6W4 · UniProt Q8A6W3
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