Research workbench
Crystal structure of R-phycoerythrin from polysiphonia at 2.8 a resolution
Analyse Crystal structure of R-phycoerythrin from polysiphonia at 2.8 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LIA
- Type
- protein
- Length
- 682 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q01921, Q01922
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, K | — | protein | 164 | — | Q01921 |
| B, L | — | protein | 177 | — | Q01922 |
Compared structures
- 1LIA · Crystal structure of R-phycoerythrin from polysiphonia at 2.8 a resolution · the same entry in another collection · chain A against A, TM-score 1.00
- Q01921 · AlphaFold monomer V2.0 prediction for R-phycoerythrin alpha chain (Q01921) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q01922 · AlphaFold monomer V2.0 prediction for R-phycoerythrin beta chain (Q01922) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q01921
- Every structure of UniProt Q01922
- Elsewhere: RCSB PDB 1LIA · PDBe 1LIA · UniProt Q01921 · UniProt Q01922
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