Research workbench
Crystal structure of TEM52 beta-lactamase
Analyse Crystal structure of TEM52 beta-lactamase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HTZ
- Type
- protein
- Length
- 1,578 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase mutant TEM52
- EC
- 3.5.2.6
- UniProt
- Q9R435
- Pockets
- 18 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Beta-lactamase mutant TEM52 (EC 3.5.2.6) | protein | 263 | 44% helix, 16% strand | Q9R435 |
Pockets
18 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1017 | 0.69 | 0.74 | 97 | empty |
| 2 | 482 | 0.59 | 0.74 | 51 | empty |
| 3 | 249 | 0.49 | 0.74 | 26 | empty |
| 4 | 228 | 0.47 | 0.74 | 27 | empty |
| 5 | 72 | 0.46 | 0.83 | 19 | empty |
Interfaces
9 interfaces between chains.
- A–D · 446 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 443 Ų buried · 8 hydrogen bonds · protein-protein
- C–E · 441 Ų buried · 7 hydrogen bonds · protein-protein
- C–F · 221 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 176 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1HTZ · Crystal structure of TEM52 beta-lactamase · 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 Q9R435
- Elsewhere: RCSB PDB 1HTZ · PDBe 1HTZ · UniProt Q9R435
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