Research workbench
Crystal structures of ribonuclease F1 of fusarium moniliforme in its free form and in complex with 2'GMP
Analyse Crystal structures of ribonuclease F1 of fusarium moniliforme in its free form… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FUT
- Type
- protein
- Length
- 106 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease F1
- EC
- 3.1.27.3
- UniProt
- P10282
- Ligands
- 2GP
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease F1 (EC 3.1.27.3) | protein | 106 | 16% helix, 26% strand | P10282 |
Ligands and binding sites
- 2GP · Guanosine-2'-monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 1FUT · Crystal structures of ribonuclease F1 of fusarium moniliforme in its free form and in… · the same entry in another collection · chain A against A, TM-score 1.00
- P10282 · AlphaFold monomer V2.0 prediction for guanyl-specific ribonuclease F1 (P10282) · 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 P10282
- Elsewhere: RCSB PDB 1FUT · PDBe 1FUT · UniProt P10282
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