Research workbench
X-ray crystal structure of human ribonuclease 4 in complex with D(UP)
Analyse X-ray crystal structure of human ribonuclease 4 in complex with D(UP) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RNF
- Type
- protein
- Length
- 240 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease 4
- EC
- 3.1.27.-
- UniProt
- P34096
- Ligands
- UM3
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribonuclease 4 (EC 3.1.27.-) | protein | 120 | 26% helix, 33% strand | P34096 |
Ligands and binding sites
- UM3 · 2'-deoxyuridine 3'-monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.60 | 0.83 | 30 | UM3 |
Interfaces
1 interface between chains.
- A–B · 649 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
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 P34096
- Elsewhere: RCSB PDB 2RNF · PDBe 2RNF · UniProt P34096
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