Research workbench
Crystal structure of mannheimia haemolytica ferric iron- binding protein a in an open conformation
Analyse Crystal structure of mannheimia haemolytica ferric iron- binding protein a in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SI1
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron binding protein fbpa
- UniProt
- Q9Z4N6
- Ligands
- FE
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Iron binding protein fbpa | protein | 316 | 44% helix, 18% strand | Q9Z4N6 |
Ligands and binding sites
- FE · Fe (III) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.45 | 0.78 | 20 | FE |
| 2 | 131 | 0.42 | 0.75 | 22 | empty |
Compared structures
- 1SI1 · Crystal Structure of Mannheimia haemolytica Ferric iron-Binding Protein A in an open… · 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 Q9Z4N6
- Elsewhere: RCSB PDB 1SI1 · PDBe 1SI1 · UniProt Q9Z4N6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.