Research workbench
Structure of a cis-proline (P114) to glycine variant of ribonuclease a
Analyse Structure of a cis-proline (P114) to glycine variant of ribonuclease a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KH8
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pancreatic ribonuclease a
- EC
- 3.1.27.5
- UniProt
- P61823
- Ligands
- CS, SO4
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pancreatic ribonuclease a (EC 3.1.27.5) | protein | 125 | 23% helix, 34% strand | P61823 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1KH8 · Structure of a cis-proline (P114) to glycine variant of Ribonuclease A · 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 1KH8 · PDBe 1KH8 · UniProt P61823
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