Research workbench
Vhh R303 C33A/C102A in complex withthe lrr domain of inlb
Analyse Vhh R303 C33A/C102A in complex withthe lrr domain of inlb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U14
- Type
- protein
- Length
- 242 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vhh R303 C33A/C102A mutant
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Vhh R303 C33A/C102A mutant | protein | 123 | 8% helix, 54% strand | — |
| A | Vhh R303 C33A/C102A mutant | protein | 119 | 6% helix, 53% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains B, A
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 | 105 | 0.38 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- B–A · 646 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6U14 · VHH R303 C33A/C102A in complex withthe LRR domain of InlB · 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
- Elsewhere: RCSB PDB 6U14 · PDBe 6U14
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