Research workbench
Cryo-EM structure of PCAT1 bound to its cta peptide substrate
Analyse Cryo-EM structure of PCAT1 bound to its cta peptide substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V9Z
- Type
- protein
- Length
- 1,472 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC-type bacteriocin transporter; Cta
- UniProt
- A3DCU1, A3DCU2
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 3 distinct chains · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ABC-type bacteriocin transporter | protein | 715 | 58% helix, 12% strand | A3DCU1 |
| C | Cta | protein | 23 | 26% helix, 9% strand | A3DCU2 |
| D | Cta | protein | 19 | 32% helix, 21% strand | A3DCU2 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 993 | 0.75 | 0.77 | 92 | empty |
| 2 | 628 | 0.73 | 0.80 | 62 | empty |
| 3 | 1008 | 0.73 | 0.76 | 89 | empty |
| 4 | 896 | 0.72 | 0.77 | 81 | empty |
| 5 | 153 | 0.71 | 0.90 | 33 | empty |
Interfaces
5 interfaces between chains.
- A–B · 5712 Ų buried · 28 hydrogen bonds · protein-protein
- A–C · 1044 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 861 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 92 Ų buried · 0 hydrogen bonds · protein-protein
- C–B · 10 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6V9Z · Cryo-EM structure of PCAT1 bound to its CtA peptide substrate · 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 A3DCU1
- Every structure of UniProt A3DCU2
- Elsewhere: RCSB PDB 6V9Z · PDBe 6V9Z · UniProt A3DCU1 · UniProt A3DCU2
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