Research workbench
Crystal structure of metallo-beta-lactamase imp-18 from pseudomonas aeruginosa
Analyse Crystal structure of metallo-beta-lactamase imp-18 from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B3R
- Type
- protein
- Length
- 433 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Imp-18
- EC
- 3.5.2.6
- UniProt
- Q5U807
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Imp-18 (EC 3.5.2.6) | protein | 214 | 28% helix, 30% strand | Q5U807 |
| B | Imp-18 (EC 3.5.2.6) | protein | 219 | 27% helix, 32% strand | Q5U807 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.51 | 0.77 | 32 | empty |
| 2 | 269 | 0.49 | 0.73 | 32 | empty |
| 3 | 190 | 0.46 | 0.74 | 33 | ZN, CIT |
| 4 | 75 | 0.29 | 0.73 | 18 | CIT |
Interfaces
1 interface between chains.
- A–B · 409 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 5B3R · Crystal structure of metallo-beta-lactamase IMP-18 from Pseudomonas aeruginosa · 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 Q5U807
- Elsewhere: RCSB PDB 5B3R · PDBe 5B3R · UniProt Q5U807
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