Research workbench
Crystal structure of CUTA1 from pyrococcus horikoshii
Analyse Crystal structure of CUTA1 from pyrococcus horikoshii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J2V
- Type
- protein
- Length
- 102 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 102AA long hypothetical periplasmic divalent cation tolerance protein cuta
- UniProt
- O58720
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 102AA long hypothetical periplasmic divalent cation tolerance protein cuta | protein | 102 | 34% helix, 37% strand | O58720 |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 1J2V · Crystal Structure of CutA1 from Pyrococcus Horikoshii · the same entry in another collection · chain A against A, TM-score 1.00
- O58720 · AlphaFold monomer V2.0 prediction for divalent-cation tolerance protein cuta (O58720) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O58720
- Elsewhere: RCSB PDB 1J2V · PDBe 1J2V · UniProt O58720
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