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Crystal structure of the type VI amidase immunity (TAI4) from agrobacterium tumefaciens
Analyse Crystal structure of the type VI amidase immunity (TAI4) from agrobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IJE
- Type
- protein
- Length
- 200 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TAI4
- UniProt
- A0A083ZID3
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 60% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | TAI4 | protein | 100 | 60% helix, 4% strand | A0A083ZID3 |
| A | TAI4 | protein | 100 | 60% helix, 4% strand | A0A083ZID3 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 7 copies · chains B, 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.38 | 0.76 | 20 | EDO |
| 2 | 83 | 0.36 | 0.76 | 22 | EDO |
Interfaces
1 interface between chains.
- B–A · 1101 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6IJE · Crystal structure of the type VI amidase immunity (Tai4) from Agrobacterium tumefaciens · the same entry in another collection · chain B against B, 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 A0A083ZID3
- Elsewhere: RCSB PDB 6IJE · PDBe 6IJE · UniProt A0A083ZID3
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