Research workbench
Structure of blac from mycobacterium tuberculosis bound to the trans- enamine adduct derived from clavulanic acid.
Analyse Structure of blac from mycobacterium tuberculosis bound to the trans- enamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H2C
- Type
- protein
- Length
- 536 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0T9EA39
- Ligands
- ISS, CO2
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 268 | — | A0A0T9EA39 |
Ligands and binding sites
- ISS · (2E)-3-[(4-hydroxy-2-oxobutyl)amino]prop-2-enal · ligand · 2 copies · chains A, B
- CO2 · Carbon dioxide · ion · chains B
- ACT · Acetate ion · additive · 4 copies · chains A, B
- 15P · Polyethylene glycol (N=34) · additive · 2 copies · chains B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6H2C · Structure of BlaC from Mycobacterium tuberculosis bound to the trans-enamine adduct… · 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 6H2C · PDBe 6H2C · UniProt A0A0T9EA39
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