MolNFT v1 · #12063 · protein
Crystal structure of human angiogenin variant Q117G
1K59: “Crystal structure of human angiogenin variant Q117G”. X-ray diffraction, 1 pocket (best druggability 0.26). MolNFT v1 #12063 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1K59
- Type
- protein
- Length
- 123 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiogenin
- EC
- 3.1.27.-
- UniProt
- P03950
- Pockets
- 1 · best druggability 0.26
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiogenin (EC 3.1.27.-) | protein | 123 | 26% helix, 36% strand | P03950 |
Ligands and binding sites
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.26 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 3 disulfide, 1 modified (disulfide, cyclization).
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 1K59 · PDBe 1K59 · UniProt P03950
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