Research workbench
Structure of a fungal protein
Analyse Structure of a fungal protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FPR
- Type
- protein
- Length
- 515 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Avirulence effector AVRLM4-7
- UniProt
- E5A6Z5
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Avirulence effector AVRLM4-7 | protein | 130 | 18% helix, 28% strand | E5A6Z5 |
| B | Avirulence effector AVRLM4-7 | protein | 128 | 19% helix, 28% strand | E5A6Z5 |
| D | Avirulence effector AVRLM4-7 | protein | 127 | 19% helix, 28% strand | E5A6Z5 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 591 | 0.77 | 0.83 | 56 | empty |
| 2 | 535 | 0.77 | 0.84 | 55 | empty |
| 3 | 649 | 0.76 | 0.82 | 76 | empty |
| 4 | 614 | 0.75 | 0.82 | 74 | empty |
| 5 | 89 | 0.33 | 0.74 | 16 | empty |
Interfaces
6 interfaces between chains.
- A–B · 920 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 848 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 781 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 780 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 66 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 4FPR · Structure of a fungal protein · 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 E5A6Z5
- Elsewhere: RCSB PDB 4FPR · PDBe 4FPR · UniProt E5A6Z5
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