Research workbench
Human activated protein C
Analyse Human activated protein C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AUT
- Type
- protein
- Length
- 338 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Activated protein C
- EC
- 3.4.21.69
- UniProt
- P04070
- Ligands
- 0G6
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Activated protein C (EC 3.4.21.69) | protein | 240 | 12% helix, 36% strand | P04070 |
| L | Activated protein C (EC 3.4.21.69) | protein | 98 | 4% helix, 24% strand | P04070 |
Ligands and binding sites
- 0G6 · D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.48 | 0.76 | 38 | 0G6 |
| 2 | 81 | 0.39 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- C–L · 896 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide, 1 covalent, 1 modified (disulfide, covalent ligand, nonstandard).
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 P04070
- Elsewhere: RCSB PDB 1AUT · PDBe 1AUT · UniProt P04070
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