Research workbench
Crystal structure of metallo beta lactamase from hirschia baltica
Analyse Crystal structure of metallo beta lactamase from hirschia baltica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V54
- Type
- protein
- Length
- 219 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase
- EC
- 3.5.2.6
- UniProt
- C6XID6
- Ligands
- ZN, MG, CL
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase (EC 3.5.2.6) | protein | 219 | 25% helix, 30% strand | C6XID6 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal
- CL · Chloride ion · ion · chains A
- FMT · Formic acid · additive · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.37 | 0.75 | 22 | FMT |
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 6V54 · Crystal Structure of Metallo Beta Lactamase from Hirschia baltica · 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 C6XID6
- Elsewhere: RCSB PDB 6V54 · PDBe 6V54 · UniProt C6XID6
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