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Binding of phosphate and pyrophosphate ions at the active site of human angiogenin as revealed by X-ray crystallography
Analyse Binding of phosphate and pyrophosphate ions at the active site of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HBY
- Type
- protein
- Length
- 123 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiogenin
- UniProt
- P03950
- Ligands
- PO4
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiogenin | protein | 123 | 24% helix, 36% strand | P03950 |
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: 3 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 1HBY · Binding of Phosphate and Pyrophosphate ions at the active site of human angiogenin as… · the same entry in another collection · chain A against A, TM-score 1.00
- P03950 · AlphaFold monomer V2.0 prediction for angiogenin (P03950) · 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 P03950
- Elsewhere: RCSB PDB 1HBY · PDBe 1HBY · UniProt P03950
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