MolNFT v1 · #12479 · protein
The X-ray structure of human angiostatin
1KI0: “The X-ray structure of human angiostatin”. X-ray diffraction, 1 ligand (BCN), 1 pocket (best druggability 0.42). MolNFT v1 #12479 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1KI0
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiostatin
- EC
- 3.4.21.7
- UniProt
- P00747
- Ligands
- BCN
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 1% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiostatin (EC 3.4.21.7) | protein | 253 | 1% helix, 17% strand | P00747 |
Ligands and binding sites
- BCN · Bicine · ligand · 3 copies · 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 | 149 | 0.42 | 0.75 | 28 | empty |
Modifications
Observed in the structure: 10 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 P00747
- Elsewhere: RCSB PDB 1KI0 · PDBe 1KI0 · UniProt P00747
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