MolNFT v1 · #110938 · protein
Rat GLUT5 with fv in the outward-open form
4YBQ · Solute carrier family 2, facilitated glucose transporter…: “Rat GLUT5 with fv in the outward-open form”. X-ray diffraction, 15 pockets (best druggability 0.86). MolNFT v1 #110938 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4YBQ
- Type
- protein
- Length
- 1,383 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Solute carrier family 2, facilitated glucose transporter member 5; Antibody fv fragment…
- UniProt
- P43427
- Pockets
- 15 · best druggability 0.86
Structure
x-ray diffraction · 5 distinct chains · 61% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Solute carrier family 2, facilitated glucose transporter member 5 | protein | 452 | 85% helix, 0% strand | P43427 |
| B | Solute carrier family 2, facilitated glucose transporter member 5 | protein | 462 | 83% helix, 0% strand | P43427 |
| C, E | Antibody fv fragment light chain | protein | 115 | 3% helix, 49% strand | — |
| D | Antibody fv fragment heavy chain | protein | 120 | 5% helix, 53% strand | — |
| F | Antibody fv fragment heavy chain | protein | 119 | 5% helix, 54% strand | — |
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1164 | 0.86 | 0.87 | 115 | empty |
| 2 | 914 | 0.82 | 0.83 | 78 | empty |
| 3 | 1058 | 0.71 | 0.75 | 77 | empty |
| 4 | 360 | 0.64 | 0.79 | 32 | empty |
| 5 | 110 | 0.64 | 0.88 | 22 | empty |
Interfaces
8 interfaces between chains.
- E–F · 977 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 956 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 630 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 597 Ų buried · 14 hydrogen bonds · protein-protein
- C–E · 438 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 P43427
- Elsewhere: RCSB PDB 4YBQ · PDBe 4YBQ · UniProt P43427
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