Research workbench
Structure of the oxidized hipip from thermochromatium tepidum at 1.4 ångström resolution
Analyse Structure of the oxidized hipip from thermochromatium tepidum at 1.4 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AMS
- Type
- protein
- Length
- 83 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High potential iron-sulfur protein
- UniProt
- P80176
- Ligands
- SF4, SO4
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High potential iron-sulfur protein | protein | 83 | 22% helix, 23% strand | P80176 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2AMS · Structure of the oxidized Hipip from thermochromatium tepidum at 1.4 angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P80176 · AlphaFold monomer V2.0 prediction for high-potential iron-sulfur protein (P80176) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P80176
- Elsewhere: RCSB PDB 2AMS · PDBe 2AMS · UniProt P80176
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