Research workbench
Crystal structure disposition of thymidylic acid tetramer in complex with ribonuclease a
Analyse Crystal structure disposition of thymidylic acid tetramer in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RTA
- Type
- protein + DNA
- Length
- 128 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'-D(*TP*TP*TP*T)-3'); Protein (ribonuclease a (E.C.3.1.27.5))
- EC
- 3.1.27.5
- UniProt
- P61823
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | DNA (5'-D(*TP*TP*TP*T)-3') | dna | 4 | — | — |
| E | Protein (ribonuclease a (E.C.3.1.27.5)) (EC 3.1.27.5) | protein | 124 | 21% helix, 34% strand | P61823 |
Interfaces
1 interface between chains.
- C–E · 576 Ų buried · 15 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1RTA · Crystal structure disposition of thymidylic acid tetramer in complex with ribonuclease a · the same entry in another collection · chain C against C, 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 P61823
- Elsewhere: RCSB PDB 1RTA · PDBe 1RTA · UniProt P61823
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.