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Crystal structure of the complex between human tissue factor extracellular domain and antibody 10H10 Fab fragment
Analyse Crystal structure of the complex between human tissue factor extracellular… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M7L
- Type
- protein
- Length
- 637 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tissue factor; 10H10 light chain; 10H10 heavy chain
- UniProt
- P13726
- Pockets
- 6 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 5% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| T | Tissue factor | protein | 194 | 8% helix, 51% strand | P13726 |
| L | 10H10 light chain | protein | 220 | 5% helix, 48% strand | — |
| H | 10H10 heavy chain | protein | 223 | 4% helix, 43% strand | — |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 650 | 0.63 | 0.74 | 66 | empty |
| 2 | 168 | 0.50 | 0.77 | 26 | empty |
| 3 | 105 | 0.47 | 0.80 | 31 | empty |
| 4 | 117 | 0.40 | 0.75 | 24 | empty |
| 5 | 75 | 0.33 | 0.75 | 20 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1977 Ų buried · 17 hydrogen bonds · protein-protein
- T–H · 743 Ų buried · 11 hydrogen bonds · protein-protein
- T–L · 494 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 4M7L · Crystal structure of the complex between human tissue factor extracellular domain and… · the same entry in another collection · chain T against T, TM-score 1.00
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 P13726
- Elsewhere: RCSB PDB 4M7L · PDBe 4M7L · UniProt P13726
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