Research workbench
Crystal structure of the protease inhibitor U-OMP19 from brucella abortus fused to maltose-binding protein
Analyse Crystal structure of the protease inhibitor U-OMP19 from brucella abortus fused… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MHW
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,OUTER membrane lipoprotein OMP19
- UniProt
- P0AEX9, Q2YLR6
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,OUTER membrane lipoprotein OMP19 | protein | 471 | 37% helix, 27% strand | P0AEX9, Q2YLR6 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A
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 | 1035 | 0.69 | 0.74 | 77 | empty |
| 2 | 83 | 0.34 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7MHW · Crystal structure of the protease inhibitor U-Omp19 from Brucella abortus fused to… · the same entry in another collection · chain A against A, TM-score 1.00
- Q2YLR6 · AlphaFold monomer V2.0 prediction for outer membrane lipoprotein OMP19 (Q2YLR6) · a predicted model of the same protein · chain A against A, TM-score 0.19
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 P0AEX9
- Every structure of UniProt Q2YLR6
- Elsewhere: RCSB PDB 7MHW · PDBe 7MHW · UniProt P0AEX9 · UniProt Q2YLR6
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