Research workbench
Crystal structure of the metallo-beta-lactamase fim-1 from pseudomonas aeruginosa in the mono-zinc form
Analyse Crystal structure of the metallo-beta-lactamase fim-1 from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V3Q
- Type
- protein
- Length
- 452 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallo-beta-lactamase fim-1
- UniProt
- K7SA42
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Metallo-beta-lactamase fim-1 | protein | 226 | 23% helix, 27% strand | K7SA42 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.57 | 0.78 | 25 | empty |
| 2 | 106 | 0.38 | 0.76 | 17 | empty |
| 3 | 78 | 0.36 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 863 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation).
Compared structures
- 6V3Q · Crystal Structure of the Metallo-beta-Lactamase FIM-1 from Pseudomonas aeruginosa in the… · 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 K7SA42
- Elsewhere: RCSB PDB 6V3Q · PDBe 6V3Q · UniProt K7SA42
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