Research workbench
1.50 ångström crystal structure of C-terminal fragment (residues 322- 384) of iron uptake system component efeo from yersinia pestis.
Analyse 1.50 ångström crystal structure of C-terminal fragment (residues 322- 384) of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TW9
- Type
- protein
- Length
- 376 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q0WFT9
- Ligands
- IOD
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, F | — | protein | 63 | — | Q0WFT9 |
| B, E | — | protein | 62 | — | Q0WFT9 |
Ligands and binding sites
- IOD · Iodide ion · ion · 17 copies · chains B, C, D, E, F
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5TW9 · 1.50 Angstrom Crystal Structure of C-terminal Fragment (residues 322-384) of Iron Uptake… · the same entry in another collection · chain F against F, TM-score 1.00
- Q0WFT9 · AlphaFold monomer V2.0 prediction for iron uptake system component efeo (Q0WFT9) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 Q0WFT9
- Elsewhere: RCSB PDB 5TW9 · PDBe 5TW9 · UniProt Q0WFT9
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