MolNFT v1 · #136520 · protein
Structure of E. COLI mce protein pqib, periplasmic domain
5UVN · Paraquat-inducible protein B: “Structure of E. COLI mce protein pqib, periplasmic domain”. Electron microscopy, 20 pockets (best druggability 0.75). MolNFT v1 #136520 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5UVN
- Type
- protein
- Length
- 2,496 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Paraquat-inducible protein B
- UniProt
- P43671
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 23% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Paraquat-inducible protein B | protein | 416 | 23% helix, 32% strand | P43671 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 974 | 0.75 | 0.78 | 112 | empty |
| 2 | 1060 | 0.74 | 0.77 | 112 | empty |
| 3 | 980 | 0.74 | 0.77 | 108 | empty |
| 4 | 433 | 0.72 | 0.82 | 35 | empty |
| 5 | 439 | 0.71 | 0.81 | 37 | empty |
Interfaces
6 interfaces between chains.
- A–F · 2071 Ų buried · 30 hydrogen bonds · protein-protein
- D–E · 2063 Ų buried · 29 hydrogen bonds · protein-protein
- E–F · 2060 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 2056 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 2053 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 5UVN · Structure of E. coli MCE protein PqiB, periplasmic domain · the same entry in another collection · chain C against C, TM-score 1.00
- P43671 · AlphaFold monomer V2.0 prediction for intermembrane transport protein pqib (P43671) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P43671
- Elsewhere: RCSB PDB 5UVN · PDBe 5UVN · UniProt P43671
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