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Crystal structure of metallo beta lactamase from erythrobacter litoralis with beta mercaptoethanol in the active site
Analyse Crystal structure of metallo beta lactamase from erythrobacter litoralis with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V73
- Type
- protein
- Length
- 228 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase II
- UniProt
- Q2N9N3
- Ligands
- ZN, CL
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase II | protein | 228 | 29% helix, 27% strand | Q2N9N3 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- BME · Beta-mercaptoethanol · additive · chains A
- FMT · Formic acid · 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 | 114 | 0.39 | 0.75 | 21 | ZN, BME |
Compared structures
- 6V73 · Crystal Structure of Metallo Beta Lactamase from Erythrobacter litoralis with beta… · 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 Q2N9N3
- Elsewhere: RCSB PDB 6V73 · PDBe 6V73 · UniProt Q2N9N3
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