Research workbench
1H and 15N sequential assignment, secondary structure and tertiary fold of [2FE-2S] ferredoxin from synechocystis sp. pcc 6803
Analyse 1H and 15N sequential assignment, secondary structure and tertiary fold of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DOX
- Type
- protein
- Length
- 96 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin [2FE-2S]
- UniProt
- P27320
- Ligands
- FES
Structure
solution nmr · 1 distinct chain · 7% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin [2FE-2S] | protein | 96 | 7% helix, 10% strand | P27320 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1DOX · 1H and 15N sequential assignment, secondary structure and tertiary fold of [2FE-2S]… · the same entry in another collection · chain A against A, TM-score 1.00
- P27320 · AlphaFold monomer V2.0 prediction for ferredoxin-1 (P27320) · a predicted model of the same protein · chain A against A, TM-score 0.50
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 P27320
- Elsewhere: RCSB PDB 1DOX · PDBe 1DOX · UniProt P27320
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