Research workbench
Human angiogenin in complex with sulphate anions at a basic solution
Analyse Human angiogenin in complex with sulphate anions at a basic solution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EPZ
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiogenin
- EC
- 3.1.27.-
- UniProt
- P03950
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiogenin (EC 3.1.27.-) | protein | 120 | 26% helix, 37% strand | P03950 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 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 P03950
- Elsewhere: RCSB PDB 5EPZ · PDBe 5EPZ · UniProt P03950
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