Research workbench
Structure of FJOH_4558, a chitin-binding susd homolog from flavobacterium johnsoniae
Analyse Structure of FJOH_4558, a chitin-binding susd homolog from flavobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5J90
- Type
- protein
- Length
- 964 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RAGB/SUSD domain protein
- UniProt
- A5FB66
- Pockets
- 14 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | RAGB/SUSD domain protein | protein | 482 | 50% helix, 5% strand | A5FB66 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.73 | 0.93 | 31 | empty |
| 2 | 55 | 0.70 | 0.98 | 20 | empty |
| 3 | 103 | 0.63 | 0.88 | 32 | empty |
| 4 | 63 | 0.61 | 0.91 | 21 | empty |
| 5 | 59 | 0.61 | 0.92 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 834 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5J90 · Structure of Fjoh_4558, a chitin-binding SusD homolog from Flavobacterium johnsoniae · 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 A5FB66
- Elsewhere: RCSB PDB 5J90 · PDBe 5J90 · UniProt A5FB66
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