Research workbench
The crytsal structure of flgd from P. aeruginosa
Analyse The crytsal structure of flgd from P. aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OSV
- Type
- protein
- Length
- 523 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar basal-body rod modification protein flgd
- UniProt
- Q9I4Q0
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 2% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar basal-body rod modification protein flgd | protein | 131 | 2% helix, 63% strand | Q9I4Q0 |
| B | Flagellar basal-body rod modification protein flgd | protein | 131 | 2% helix, 62% strand | Q9I4Q0 |
| C | Flagellar basal-body rod modification protein flgd | protein | 132 | 2% helix, 61% strand | Q9I4Q0 |
| D | Flagellar basal-body rod modification protein flgd | protein | 129 | 2% helix, 64% strand | Q9I4Q0 |
Ligands and binding sites
- GOL · Glycerol · additive · 10 copies · chains A, D, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1010 | 0.73 | 0.76 | 81 | GOL |
| 2 | 85 | 0.33 | 0.74 | 22 | empty |
| 3 | 63 | 0.32 | 0.75 | 18 | empty |
| 4 | 54 | 0.30 | 0.75 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1437 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 331 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 325 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3OSV · The crytsal structure of FLGD from P. Aeruginosa · 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 Q9I4Q0
- Elsewhere: RCSB PDB 3OSV · PDBe 3OSV · UniProt Q9I4Q0
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