Research workbench
Ompt (in-vitro folded), an outer membrane protein vibrio cholerae (trimer form)
Analyse Ompt (in-vitro folded), an outer membrane protein vibrio cholerae (trimer form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EHF
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ompt protein
- UniProt
- A0A0H3AME7
- Ligands
- CA
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 69% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ompt protein | protein | 318 | 3% helix, 69% strand | A0A0H3AME7 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 408 | 0.63 | 0.78 | 55 | empty |
| 2 | 399 | 0.56 | 0.74 | 53 | empty |
| 3 | 244 | 0.53 | 0.76 | 29 | empty |
Compared structures
- 6EHF · OmpT (in-vitro folded), an outer membrane protein Vibrio cholerae (trimer form) · 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 A0A0H3AME7
- Elsewhere: RCSB PDB 6EHF · PDBe 6EHF · UniProt A0A0H3AME7
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