Research workbench
Crystal structure of the triscatecholate siderophore binding protein feua from bacillus subtilis complexed with ferric mecam
Analyse Crystal structure of the triscatecholate siderophore binding protein feua from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XV1
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron-uptake system-binding protein
- UniProt
- P40409
- Ligands
- ECA, FE, PO4
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Iron-uptake system-binding protein | protein | 283 | 40% helix, 20% strand | P40409 |
Ligands and binding sites
- ECA · N,N',N''-[benzene-1,3,5-triyltris(methylene)]tris(2,3-dihydroxybenzamide) · ligand · chains A
- FE · Fe (III) ion · metal · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.53 | 0.79 | 29 | ECA, FE |
Compared structures
- 2XV1 · Crystal structure of the triscatecholate siderophore binding protein FeuA from Bacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- P40409 · AlphaFold monomer V2.0 prediction for iron-uptake system-binding protein (P40409) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P40409
- Elsewhere: RCSB PDB 2XV1 · PDBe 2XV1 · UniProt P40409
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