Research workbench
Crystal structure of beta-lactamase penp mutant-E166H
Analyse Crystal structure of beta-lactamase penp mutant-E166H in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GHX
- Type
- protein
- Length
- 513 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase
- EC
- 3.5.2.6
- UniProt
- P00808
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase (EC 3.5.2.6) | protein | 257 | 42% helix, 19% strand | P00808 |
| B | Beta-lactamase (EC 3.5.2.6) | protein | 256 | 43% helix, 19% strand | P00808 |
Ligands and binding sites
- ACY · Acetic acid · additive · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
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 | 1167 | 0.74 | 0.77 | 108 | ACY |
| 2 | 81 | 0.44 | 0.80 | 17 | empty |
| 3 | 67 | 0.43 | 0.82 | 17 | empty |
| 4 | 95 | 0.32 | 0.73 | 26 | ACY |
Interfaces
1 interface between chains.
- A–B · 607 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 P00808
- Elsewhere: RCSB PDB 5GHX · PDBe 5GHX · UniProt P00808
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