Research workbench
Crystal structure of prethrombin-2 mutant E14EA/D14LA/E18A/S195A
Analyse Crystal structure of prethrombin-2 mutant E14EA/D14LA/E18A/S195A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H6T
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prothrombin
- EC
- 3.4.21.5
- UniProt
- P00734
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prothrombin (EC 3.4.21.5) | protein | 293 | 17% helix, 31% strand | P00734 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 7 copies · 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 | 113 | 0.52 | 0.82 | 26 | empty |
| 2 | 58 | 0.38 | 0.79 | 13 | empty |
| 3 | 79 | 0.33 | 0.74 | 22 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4H6T · Crystal structure of prethrombin-2 mutant E14eA/D14lA/E18A/S195A · the same entry in another collection · chain A against A, 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 P00734
- Elsewhere: RCSB PDB 4H6T · PDBe 4H6T · UniProt P00734
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