MolNFT v1 · #12588 · protein
Crystal structure of uninhibited factor viia
1KLJ: “Crystal structure of uninhibited factor viia”. X-ray diffraction, 1 ligand (CA), 4 pockets (best druggability 0.46). MolNFT v1 #12588 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1KLJ
- Type
- protein
- Length
- 304 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Factor viia
- EC
- 3.4.21.21
- UniProt
- P08709
- Ligands
- CA
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Factor viia (EC 3.4.21.21) | protein | 56 | 14% helix, 29% strand | P08709 |
| H | Factor viia (EC 3.4.21.21) | protein | 248 | 14% helix, 35% strand | P08709 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.46 | 0.76 | 21 | empty |
| 2 | 52 | 0.42 | 0.82 | 14 | empty |
| 3 | 106 | 0.37 | 0.75 | 30 | empty |
| 4 | 53 | 0.36 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- L–H · 1015 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 P08709
- Elsewhere: RCSB PDB 1KLJ · PDBe 1KLJ · UniProt P08709
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