Research workbench
Trichodesmium TERY_3377 (idia) (futa) with iron and alanine ligand.
Analyse Trichodesmium TERY_3377 (idia) (futa) with iron and alanine ligand. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G7N
- Type
- protein
- Length
- 638 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Extracellular solute-binding protein, family 1
- UniProt
- Q10Z45
- Ligands
- DAL, DGL, FE
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Extracellular solute-binding protein, family 1 | protein | 318 | 47% helix, 18% strand | Q10Z45 |
| B | Extracellular solute-binding protein, family 1 | protein | 320 | 47% helix, 18% strand | Q10Z45 |
Ligands and binding sites
- DAL · D-alanine · ligand · chains A
- DGL · D-glutamic acid · ligand · chains A
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.67 | 0.77 | 69 | empty |
| 2 | 259 | 0.64 | 0.81 | 34 | empty |
| 3 | 83 | 0.32 | 0.74 | 20 | DAL, DGL |
Interfaces
1 interface between chains.
- A–B · 797 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 d-amino (D-amino acid).
Compared structures
- 6G7N · Trichodesmium Tery_3377 (IdiA) (FutA) with iron and alanine ligand. · 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 Q10Z45
- Elsewhere: RCSB PDB 6G7N · PDBe 6G7N · UniProt Q10Z45
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