Research workbench
Crystal structure of hsc K148E
Analyse Crystal structure of hsc K148E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TE0
- Type
- protein
- Length
- 1,293 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FORMATE/NITRITE transporter
- UniProt
- Q186B7
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | FORMATE/NITRITE transporter | protein | 257 | 82% helix, 0% strand | Q186B7 |
| C | FORMATE/NITRITE transporter | protein | 266 | 79% helix, 0% strand | Q186B7 |
| E | FORMATE/NITRITE transporter | protein | 256 | 82% helix, 0% strand | Q186B7 |
Ligands and binding sites
- BOG · octyl beta-D-glucopyranoside · additive · 4 copies · chains A, B, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 918 | 0.79 | 0.80 | 66 | empty |
| 2 | 334 | 0.67 | 0.81 | 38 | empty |
| 3 | 332 | 0.66 | 0.81 | 40 | empty |
| 4 | 342 | 0.66 | 0.80 | 41 | empty |
| 5 | 349 | 0.65 | 0.80 | 43 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1718 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 1651 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1565 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 1562 Ų buried · 11 hydrogen bonds · protein-protein
- C–E · 1557 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3TE0 · Crystal structure of HSC K148E · 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 Q186B7
- Elsewhere: RCSB PDB 3TE0 · PDBe 3TE0 · UniProt Q186B7
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