Research workbench
Crystal structure of ppca V13T mutant
Analyse Crystal structure of ppca V13T mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HC3
- Type
- protein
- Length
- 71 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ppca
- UniProt
- Q8GGK7
- Ligands
- HEC, DXC, SO4
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ppca | protein | 71 | 42% helix, 10% strand | Q8GGK7 |
Ligands and binding sites
- HEC · Heme C · ligand · 3 copies · chains A
- DXC · (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 505 | 0.66 | 0.77 | 46 | HEC, DXC |
Modifications
Observed in the structure: 6 cofactor (heme c attachment).
Compared structures
- 4HC3 · Crystal structure of PpcA V13T mutant · 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 Q8GGK7
- Elsewhere: RCSB PDB 4HC3 · PDBe 4HC3 · UniProt Q8GGK7
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