Research workbench
Crystal structure of tem-1 beta-lactamase mutant M182N
Analyse Crystal structure of tem-1 beta-lactamase mutant M182N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B2N
- Type
- protein
- Length
- 1,033 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase tem
- EC
- 3.5.2.6
- UniProt
- P62593
- Ligands
- SO4
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase tem (EC 3.5.2.6) | protein | 260 | 42% helix, 15% strand | P62593 |
| B | Beta-lactamase tem (EC 3.5.2.6) | protein | 255 | 42% helix, 11% strand | P62593 |
| C | Beta-lactamase tem (EC 3.5.2.6) | protein | 257 | 46% helix, 16% strand | P62593 |
| D | Beta-lactamase tem (EC 3.5.2.6) | protein | 261 | 44% helix, 15% strand | P62593 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 604 | 0.71 | 0.79 | 37 | empty |
| 2 | 492 | 0.62 | 0.76 | 58 | SO4 |
| 3 | 198 | 0.61 | 0.82 | 24 | empty |
| 4 | 258 | 0.61 | 0.80 | 41 | empty |
| 5 | 246 | 0.53 | 0.77 | 27 | empty |
Interfaces
4 interfaces between chains.
- A–B · 678 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 480 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 241 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 52 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 P62593
- Elsewhere: RCSB PDB 6B2N · PDBe 6B2N · UniProt P62593
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