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Cryo-EM structure of the proton coupled folate transporter at pH 6.0 bound to pemetrexed
Analyse Cryo-EM structure of the proton coupled folate transporter at pH 6.0 bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BC7
- Type
- protein
- Length
- 549 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proton-coupled folate transporter; Nanobody
- UniProt
- E6Y8U5
- Ligands
- LYA
- Pockets
- 4 · best druggability 0.84
Structure
electron microscopy · 2 distinct chains · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proton-coupled folate transporter | protein | 432 | 74% helix, 0% strand | E6Y8U5 |
| B | Nanobody | protein | 117 | 3% helix, 38% strand | — |
Ligands and binding sites
- LYA · 2-{4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)-ethyl]-benzoylamino}-pentanedioic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1191 | 0.84 | 0.85 | 105 | LYA |
| 2 | 221 | 0.55 | 0.78 | 35 | empty |
| 3 | 53 | 0.44 | 0.84 | 17 | empty |
| 4 | 57 | 0.29 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1081 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 7BC7 · Cryo-EM structure of the proton coupled folate transporter at pH 6.0 bound to pemetrexed · 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 E6Y8U5
- Elsewhere: RCSB PDB 7BC7 · PDBe 7BC7 · UniProt E6Y8U5
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