Research workbench
Solution NMR structure of the periplasmic signaling domain of the outer membrane iron transporter feca from escherichia COLI.
Analyse Solution NMR structure of the periplasmic signaling domain of the outer… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZZV
- Type
- protein
- Length
- 80 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IRON(III) dicitrate transport protein feca
- UniProt
- P13036
Structure
solution nmr · 1 distinct chain · 25% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | IRON(III) dicitrate transport protein feca | protein | 80 | 25% helix, 24% strand | P13036 |
Compared structures
- 1ZZV · Solution NMR Structure of the Periplasmic Signaling Domain of the Outer Membrane Iron… · the same entry in another collection · chain A against A, TM-score 1.00
- P13036 · AlphaFold monomer V2.0 prediction for FE(3+) dicitrate transport protein feca (P13036) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 P13036
- Elsewhere: RCSB PDB 1ZZV · PDBe 1ZZV · UniProt P13036
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