Research workbench
Crystal structure of hsc F194I
Analyse Crystal structure of hsc F194I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TDS
- 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 0.80
Structure
x-ray diffraction · 3 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | FORMATE/NITRITE transporter | protein | 256 | 81% helix, 0% strand | Q186B7 |
| A, B, D | FORMATE/NITRITE transporter | protein | 257 | 82% helix, 0% strand | Q186B7 |
| C | FORMATE/NITRITE transporter | protein | 266 | 78% helix, 0% strand | Q186B7 |
Ligands and binding sites
- BOG · octyl beta-D-glucopyranoside · additive · 5 copies · chains E, A, B, C, D
- PG4 · Tetraethylene glycol · additive · 4 copies · chains E, C, A, B, D
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 | 1089 | 0.80 | 0.81 | 75 | BOG |
| 2 | 433 | 0.66 | 0.79 | 41 | empty |
| 3 | 316 | 0.65 | 0.81 | 36 | PG4 |
| 4 | 325 | 0.65 | 0.80 | 40 | empty |
| 5 | 320 | 0.64 | 0.80 | 40 | PG4 |
Interfaces
5 interfaces between chains.
- C–D · 1700 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 1651 Ų buried · 12 hydrogen bonds · protein-protein
- E–B · 1650 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1593 Ų buried · 10 hydrogen bonds · protein-protein
- E–C · 1549 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 3TDS · Crystal structure of HSC F194I · the same entry in another collection · chain E against E, 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 3TDS · PDBe 3TDS · UniProt Q186B7
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