MolNFT v1 · #109824 · protein
Coagulation factor XII protease domain crystal structure
4XE4: “Coagulation factor XII protease domain crystal structure”. X-ray diffraction, 1 ligand (NAG), 3 pockets (best druggability 0.63). MolNFT v1 #109824 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4XE4
- Type
- protein
- Length
- 231 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coagulation factor XII
- EC
- 3.4.21.38
- UniProt
- P00748
- Ligands
- NAG
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coagulation factor XII (EC 3.4.21.38) | protein | 231 | 11% helix, 35% strand | P00748 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- GOL · Glycerol · additive · chains A
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 | 187 | 0.63 | 0.84 | 33 | empty |
| 2 | 100 | 0.40 | 0.76 | 15 | empty |
| 3 | 54 | 0.29 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).
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 P00748
- Elsewhere: RCSB PDB 4XE4 · PDBe 4XE4 · UniProt P00748
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