MolNFT v1 · #20702 · protein
HIS92ALA mutation in ribonuclease T1 induces segmental flexibility. an X-ray study
1RN4: “HIS92ALA mutation in ribonuclease T1 induces segmental flexibility. an X-ray study”. X-ray diffraction, 1 ligand (PO4). MolNFT v1 #20702 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RN4
- Type
- protein
- Length
- 100 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease T1
- EC
- 3.1.27.3
- UniProt
- P00651
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease T1 (EC 3.1.27.3) | protein | 100 | 17% helix, 33% strand | P00651 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1RN4 · HIS92ALA mutation in ribonuclease T1 induces segmental flexibility. an X-ray study · 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 P00651
- Elsewhere: RCSB PDB 1RN4 · PDBe 1RN4 · UniProt P00651
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