Research workbench
Human factor viia-tissue factor in complex with peptide-mimetic inhibitor that has two charged groups in P2 and P4
Analyse Human factor viia-tissue factor in complex with peptide-mimetic inhibitor that… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WSS
- Type
- protein
- Length
- 587 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coagulation factor VII; Tissue factor
- EC
- 3.4.21.21
- UniProt
- P08709, P13726
- Ligands
- 3CB, BGC, FUC, CA
- Pockets
- 8 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 14% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Coagulation factor VII (EC 3.4.21.21) | protein | 142 | 25% helix, 18% strand | P08709 |
| H | Coagulation factor VII (EC 3.4.21.21) | protein | 254 | 13% helix, 37% strand | P08709 |
| T | Tissue factor | protein | 191 | 8% helix, 51% strand | P13726 |
Ligands and binding sites
- 3CB · N-[(3-carboxybenzyl)sulfonyl]isoleucyl-N~1~-{4-[amino(imino)methyl]benzyl}-5-iminoornithinamide · ligand · chains H
- BGC · beta-D-glucopyranose · sugar · chains L
- FUC · alpha-L-fucopyranose · sugar · chains L, T
- CA · Calcium ion · metal · 9 copies · chains L, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 365 | 0.63 | 0.79 | 49 | empty |
| 2 | 84 | 0.50 | 0.83 | 17 | empty |
| 3 | 121 | 0.50 | 0.80 | 27 | empty |
| 4 | 112 | 0.47 | 0.79 | 22 | empty |
| 5 | 157 | 0.46 | 0.76 | 33 | 3CB |
Interfaces
3 interfaces between chains.
- L–T · 1439 Ų buried · 16 hydrogen bonds · protein-protein
- L–H · 1020 Ų buried · 15 hydrogen bonds · protein-protein
- H–T · 585 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 10 modified, 2 glycan (disulfide, carboxylation, O-glycosylation).
Compared structures
- 1WSS · Human Factor Viia-Tissue Factor in Complex with peptide-mimetic inhibitor that has two… · the same entry in another collection · chain L against L, TM-score 1.00
- P13726 · AlphaFold monomer V2.0 prediction for tissue factor (P13726) · a predicted model of the same protein · chain T against A, TM-score 0.99
- P08709 · AlphaFold monomer V2.0 prediction for coagulation factor VII (P08709) · a predicted model of the same protein · chain H against A, TM-score 0.97
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
- Every structure of UniProt P13726
- Elsewhere: RCSB PDB 1WSS · PDBe 1WSS · UniProt P08709 · UniProt P13726
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