Research workbench
1.99 a resolution structure of semet-CT263 (mtan) from chlamydia trachomatis
Analyse 1.99 a resolution structure of semet-CT263 (mtan) from chlamydia trachomatis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QFB
- Type
- protein
- Length
- 382 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CT263
- UniProt
- B0B7H9
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CT263 | protein | 195 | 28% helix, 34% strand | B0B7H9 |
| B | CT263 | protein | 187 | 28% helix, 33% strand | B0B7H9 |
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 | 198 | 0.57 | 0.80 | 23 | empty |
| 2 | 192 | 0.49 | 0.76 | 25 | empty |
| 3 | 185 | 0.48 | 0.76 | 28 | empty |
| 4 | 183 | 0.46 | 0.75 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 571 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 4QFB · 1.99 A resolution structure of SeMet-CT263 (MTAN) from Chlamydia trachomatis · 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 B0B7H9
- Elsewhere: RCSB PDB 4QFB · PDBe 4QFB · UniProt B0B7H9
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