Research workbench
Crystal structure of AVR4 (R112L/C122S)-bna complex
Analyse Crystal structure of AVR4 (R112L/C122S)-bna complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OFB
- Type
- protein
- Length
- 239 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Avidin-related protein 4/5
- UniProt
- P56734
- Ligands
- BNI
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Avidin-related protein 4/5 | protein | 120 | 8% helix, 50% strand | P56734 |
| B | Avidin-related protein 4/5 | protein | 119 | 8% helix, 50% strand | P56734 |
Ligands and binding sites
- BNI · 5-(2-oxo-hexahydro-thieno[3,4-d]imidazol-6-yl)-pentanoic acid (4-nitro-phenyl)-amide · ligand · 2 copies · chains A, B
- FMT · Formic acid · additive · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.51 | 0.80 | 21 | BNI |
| 2 | 141 | 0.50 | 0.79 | 21 | BNI |
Interfaces
1 interface between chains.
- A–B · 1678 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 P56734
- Elsewhere: RCSB PDB 2OFB · PDBe 2OFB · UniProt P56734
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