MolNFT v1 · #12587 · protein
Cofactor-and substrate-assisted activation of factor viia
1KLI: “Cofactor-and substrate-assisted activation of factor viia”. X-ray diffraction, 3 ligands (BEN, CA, SO4), 3 pockets (best druggability 0.53). MolNFT v1 #12587 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1KLI
- Type
- protein
- Length
- 315 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
- BEN, CA, SO4
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Factor viia (EC 3.4.21.21) | protein | 61 | 13% helix, 26% strand | P08709 |
| H | Factor viia (EC 3.4.21.21) | protein | 254 | 14% helix, 37% strand | P08709 |
Ligands and binding sites
- BEN · Benzamidine · ligand · chains H
- CA · Calcium ion · metal · chains H
- SO4 · Sulfate ion · ion · 4 copies · chains H
- GOL · Glycerol · additive · chains H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.53 | 0.83 | 17 | SO4 |
| 2 | 113 | 0.39 | 0.75 | 17 | empty |
| 3 | 105 | 0.39 | 0.76 | 29 | SO4, BEN |
Interfaces
1 interface between chains.
- L–H · 1043 Ų buried · 15 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 1KLI · PDBe 1KLI · UniProt P08709
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