Research workbench
Structure of S70A blac from mycobacterium tuberculosis obtained from crystals produced in the absence of dtt
Analyse Structure of S70A blac from mycobacterium tuberculosis obtained from crystals… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H28
- Type
- protein
- Length
- 541 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase
- EC
- 3.5.2.6
- UniProt
- A0A0T9EA39
- Pockets
- 4 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase (EC 3.5.2.6) | protein | 271 | 45% helix, 17% strand | A0A0T9EA39 |
| B | Beta-lactamase (EC 3.5.2.6) | protein | 270 | 46% helix, 17% strand | A0A0T9EA39 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, B
- 15P · Polyethylene glycol (N=34) · additive · chains A
- GOL · Glycerol · additive · chains 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.48 | 0.73 | 39 | empty |
| 2 | 166 | 0.48 | 0.76 | 16 | empty |
| 3 | 146 | 0.43 | 0.75 | 21 | PEG |
| 4 | 140 | 0.40 | 0.74 | 22 | PEG |
Interfaces
1 interface between chains.
- A–B · 263 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6H28 · Structure of S70A BlaC from Mycobacterium tuberculosis obtained from crystals produced in… · 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 A0A0T9EA39
- Elsewhere: RCSB PDB 6H28 · PDBe 6H28 · UniProt A0A0T9EA39
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