Research workbench
Auracyanin, a blue copper protein from the green thermophilic photosynthetic bacterium chloroflexus aurantiacus
Analyse Auracyanin, a blue copper protein from the green thermophilic photosynthetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QHQ
- Type
- protein
- Length
- 139 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (auracyanin)
- UniProt
- P27197
- Ligands
- CU, SO4, CL
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (auracyanin) | protein | 139 | 11% helix, 38% strand | P27197 |
Ligands and binding sites
- CU · Copper (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1QHQ · Auracyanin, a blue copper protein from the green thermophilic photosynthetic bacterium… · the same entry in another collection · chain A against A, TM-score 1.00
- P27197 · AlphaFold monomer V2.0 prediction for auracyanin-B (P27197) · a predicted model of the same protein · 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 P27197
- Elsewhere: RCSB PDB 1QHQ · PDBe 1QHQ · UniProt P27197
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