Research workbench
Crystal structure of peptidylprolyl isomerase from naegleria fowleri
Analyse Crystal structure of peptidylprolyl isomerase from naegleria fowleri in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B4P
- Type
- protein
- Length
- 232 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidylprolyl isomerase
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidylprolyl isomerase | protein | 117 | 13% helix, 38% strand | — |
| B | Peptidylprolyl isomerase | protein | 115 | 13% helix, 38% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.35 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 634 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6B4P · Crystal Structure of Peptidylprolyl Isomerase from Naegleria fowleri · 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
- Elsewhere: RCSB PDB 6B4P · PDBe 6B4P
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