Research workbench
Crystal Structure of TTHA0252 from Thermus thermophilus HB8 complexed with UMP
Analyse Crystal Structure of TTHA0252 from Thermus thermophilus HB8 complexed with UMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IEL
- Type
- protein
- Length
- 1,724 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.35
- Source
- Thermus thermophilus
- UniProt
- Q5SLP1
Structure
x-ray diffraction · resolution 2.35 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 431 | — | Q5SLP1 |
Compared structures
- 3IEL · Crystal structure of TTHA0252 from thermus thermophilus HB8 complexed with ump · the same entry in another collection · chain A against A, TM-score 1.00
- Q5SLP1 · AlphaFold monomer V2.0 prediction for ribonuclease TTHA0252 (Q5SLP1) · a predicted model of the same protein · chain A 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 Q5SLP1
- Elsewhere: RCSB PDB 3IEL · PDBe 3IEL · UniProt Q5SLP1
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