Research workbench
C-terminal region of the xanthomonas campestris pv. campestris old protein phased with iodine
Analyse C-terminal region of the xanthomonas campestris pv. campestris old protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NJV
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- XCC_CTR_I
- UniProt
- B0RTN2
- Ligands
- MG, IOD
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | XCC_CTR_I | protein | 206 | 59% helix, 10% strand | B0RTN2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.27 | 0.73 | 15 | empty |
Compared structures
- 6NJV · C-terminal region of the Xanthomonas campestris pv. campestris OLD protein phased with… · 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 B0RTN2
- Elsewhere: RCSB PDB 6NJV · PDBe 6NJV · UniProt B0RTN2
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