Research workbench
The crystal structure of a novel electron transfer ferredoxin from R. palustris HAA2
Analyse The crystal structure of a novel electron transfer ferredoxin from R. palustris… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OV1
- Type
- protein
- Length
- 66 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative ferredoxin
- UniProt
- Q2ITY5
- Ligands
- F3S
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ferredoxin | protein | 66 | 27% helix, 26% strand | Q2ITY5 |
Ligands and binding sites
- F3S · FE3-S4 cluster · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4OV1 · The crystal structure of a novel electron transfer ferredoxin from R. palustris HaA2 · 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 Q2ITY5
- Elsewhere: RCSB PDB 4OV1 · PDBe 4OV1 · UniProt Q2ITY5
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