MolNFT v1 · #5007 · protein
Anion-selective porin from comamonas acidovorans
1E54 · Outer membrane porin protein 32: “Anion-selective porin from comamonas acidovorans”. X-ray diffraction, 2 ligands (CA, SO4), 2 pockets (best druggability 0.65). MolNFT v1 #5007 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1E54
- Type
- protein
- Length
- 340 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer membrane porin protein 32; OMP32
- UniProt
- P24305
- Ligands
- CA, SO4
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer membrane porin protein 32 | protein | 332 | 4% helix, 58% strand | P24305 |
| B | OMP32 | protein | 8 | 0% helix, 25% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 548 | 0.65 | 0.76 | 61 | SO4 |
| 2 | 54 | 0.28 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 402 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (cyclization).
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 P24305
- Elsewhere: RCSB PDB 1E54 · PDBe 1E54 · UniProt P24305
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