Research workbench
Crystal structure of pf-PCP(1-204)-C
Analyse Crystal structure of pf-PCP(1-204)-C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DF5
- Type
- protein
- Length
- 852 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyrrolidone-carboxylate peptidase
- EC
- 3.4.19.3
- UniProt
- O73944
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Pyrrolidone-carboxylate peptidase (EC 3.4.19.3) | protein | 213 | 36% helix, 23% strand | O73944 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1043 | 0.78 | 0.80 | 82 | empty |
| 2 | 766 | 0.76 | 0.81 | 71 | empty |
| 3 | 72 | 0.43 | 0.80 | 14 | empty |
| 4 | 82 | 0.35 | 0.75 | 16 | empty |
| 5 | 75 | 0.34 | 0.75 | 14 | empty |
Interfaces
5 interfaces between chains.
- A–C · 756 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 746 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 682 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 662 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 155 Ų buried · 2 hydrogen bonds · protein-protein
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 O73944
- Elsewhere: RCSB PDB 2DF5 · PDBe 2DF5 · UniProt O73944
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