MolNFT v1 · #86325 · protein
Crystal structure of human angiogenin with an engineered loop exhibits conformational flexibility at the functional regions of the molecule
4B36 · Angiogenin, eosinophil cationic-related protein: “Crystal structure of human angiogenin with an engineered loop exhibits conformational flexibility at the…”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.44).…
- PDB
- 4B36
- Type
- protein
- Length
- 228 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiogenin, eosinophil cationic-related protein
- EC
- 3.1.27.-
- UniProt
- P03950, Q12762
- Ligands
- CL
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiogenin, eosinophil cationic-related protein (EC 3.1.27.-) | protein | 116 | 28% helix, 31% strand | P03950, Q12762 |
| B | Angiogenin, eosinophil cationic-related protein (EC 3.1.27.-) | protein | 112 | 28% helix, 34% strand | P03950, Q12762 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.44 | 0.75 | 26 | empty |
| 2 | 96 | 0.37 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 190 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 4B36 · Crystal Structure of Human Angiogenin with an Engineered Loop Exhibits Conformational… · 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 B against A, TM-score 0.91
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
- Every structure of UniProt Q12762
- Elsewhere: RCSB PDB 4B36 · PDBe 4B36 · UniProt P03950 · UniProt Q12762
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