MolNFT v1 · #4453 · protein
2FE-2S ferredoxin from haloarcula marismortui
1DOI: “2FE-2S ferredoxin from haloarcula marismortui”. X-ray diffraction, 2 ligands (FES, K). MolNFT v1 #4453 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DOI
- Type
- protein
- Length
- 128 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2FE-2S ferredoxin
- UniProt
- P00217
- Ligands
- FES, K
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2FE-2S ferredoxin | protein | 128 | 30% helix, 25% strand | P00217 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P00217
- Elsewhere: RCSB PDB 1DOI · PDBe 1DOI · UniProt P00217
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