Research workbench
Crystal structure of hsc T84A
Analyse Crystal structure of hsc T84A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TE1
- 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
- 18 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | FORMATE/NITRITE transporter | protein | 257 | 81% helix, 0% strand | Q186B7 |
| C | FORMATE/NITRITE transporter | protein | 266 | 75% helix, 0% strand | Q186B7 |
| E | FORMATE/NITRITE transporter | protein | 256 | 81% helix, 0% strand | Q186B7 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 4 copies · chains A, B, D, C, E
- BOG · octyl beta-D-glucopyranoside · additive · 2 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1059 | 0.80 | 0.81 | 78 | BOG |
| 2 | 338 | 0.67 | 0.81 | 43 | PG4 |
| 3 | 392 | 0.66 | 0.80 | 46 | empty |
| 4 | 372 | 0.65 | 0.79 | 32 | empty |
| 5 | 300 | 0.65 | 0.81 | 35 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1687 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 1681 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 1643 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1585 Ų buried · 8 hydrogen bonds · protein-protein
- C–E · 1570 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3TE1 · Crystal structure of HSC T84A · 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 3TE1 · PDBe 3TE1 · UniProt Q186B7
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