Research workbench
Cryo-EM structure of PDR5 from saccharomyces cerevisiae in inward- facing conformation with ADP/ATP
Analyse Cryo-EM structure of PDR5 from saccharomyces cerevisiae in inward- facing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P04
- Type
- protein
- Length
- 1,353 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pleiotropic ABC efflux transporter of multiple drugs
- UniProt
- P33302
- Ligands
- ATP, ADP
- Pockets
- 15 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pleiotropic ABC efflux transporter of multiple drugs | protein | 1353 | 55% helix, 11% strand | P33302 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1006 | 0.85 | 0.86 | 75 | empty |
| 2 | 668 | 0.79 | 0.84 | 87 | ATP |
| 3 | 147 | 0.79 | 0.96 | 35 | empty |
| 4 | 549 | 0.74 | 0.81 | 38 | empty |
| 5 | 166 | 0.58 | 0.82 | 25 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7P04 · Cryo-EM structure of Pdr5 from Saccharomyces cerevisiae in inward-facing conformation… · the same entry in another collection · chain A against A, TM-score 1.00
- P33302 · AlphaFold monomer V2.0 prediction for pleiotropic ABC efflux transporter of multiple… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P33302
- Elsewhere: RCSB PDB 7P04 · PDBe 7P04 · UniProt P33302
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