MolNFT v1 · #143819 · protein
Crystal structure of thermus thermophilus rod shape determining protein roda D255A mutant (Q5SIX3_THET8)
6BAS · Peptidoglycan glycosyltransferase roda: “Crystal structure of thermus thermophilus rod shape determining protein roda D255A mutant (Q5SIX3_THET8)”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.68). MolNFT v1…
- PDB
- 6BAS
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidoglycan glycosyltransferase roda
- EC
- 2.4.1.129
- UniProt
- Q5SIX3
- Ligands
- CL
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan glycosyltransferase roda (EC 2.4.1.129) | protein | 298 | 68% helix, 3% strand | Q5SIX3 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 549 | 0.68 | 0.78 | 71 | empty |
| 2 | 150 | 0.51 | 0.78 | 17 | empty |
Compared structures
- 6BAS · Crystal structure of Thermus thermophilus Rod shape determining protein RodA D255A mutant… · 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 Q5SIX3
- Elsewhere: RCSB PDB 6BAS · PDBe 6BAS · UniProt Q5SIX3
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