Research workbench
Water dependent domain motion and flexibility in ribonuclease a and the invariant features in its hydration shell. an X-ray study of two low humidity crystal forms of the enzyme
Analyse Water dependent domain motion and flexibility in ribonuclease a and the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RHB
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease a
- EC
- 3.1.27.5
- UniProt
- P61823
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease a (EC 3.1.27.5) | protein | 124 | 21% helix, 35% strand | P61823 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1RHB · Water dependent domain motion and flexibility in ribonuclease a and the invariant… · the same entry in another collection · 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 P61823
- Elsewhere: RCSB PDB 1RHB · PDBe 1RHB · UniProt P61823
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