MolNFT v1 · #172347 · protein
Crystal structure of the cubic catalytic core of the mycobacterium tuberculosis branched-chain alphaketoacid acyltransferase component (E2B).
6ZZN · Dihydrolipoyllysine-residue acyltransferase component of…: “Crystal structure of the cubic catalytic core of the mycobacterium tuberculosis branched-chain alphaketoacid…”. X-ray diffraction, 4 pockets (best druggability 0.59).…
- PDB
- 6ZZN
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid…
- EC
- 2.3.1.168
- UniProt
- O06159
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex (EC 2.3.1.168) | protein | 224 | 42% helix, 26% strand | O06159 |
Ligands and binding sites
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 | 126 | 0.59 | 0.84 | 23 | empty |
| 2 | 106 | 0.37 | 0.74 | 22 | empty |
| 3 | 81 | 0.37 | 0.76 | 21 | empty |
| 4 | 65 | 0.33 | 0.76 | 12 | empty |
Compared structures
- 6ZZN · Crystal structure of the cubic catalytic core of the Mycobacterium tuberculosis… · the same entry in another collection · chain A against A, TM-score 1.00
- O06159 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O06159
- Elsewhere: RCSB PDB 6ZZN · PDBe 6ZZN · UniProt O06159
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