Research workbench
Crystal structure of PRGX/CCF10 complex
Analyse Crystal structure of PRGX/CCF10 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AXZ
- Type
- protein
- Length
- 1,224 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prgx; Lvtlvfv peptide; TPPKEVT(MSE) peptide
- UniProt
- Q04114
- Pockets
- 16 · best druggability 0.79
Structure
x-ray diffraction · 5 distinct chains · 67% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prgx | protein | 306 | 66% helix, 2% strand | Q04114 |
| B, D | Prgx | protein | 305 | 67% helix, 2% strand | Q04114 |
| C | Prgx | protein | 279 | 71% helix, 0% strand | Q04114 |
| E, F, H | Lvtlvfv peptide | protein | 7 | 0% helix, 29% strand | — |
| I | TPPKEVT(MSE) peptide | protein | 8 | 0% helix, 0% strand | — |
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1163 | 0.79 | 0.80 | 115 | empty |
| 2 | 117 | 0.79 | 0.98 | 22 | empty |
| 3 | 434 | 0.77 | 0.86 | 72 | empty |
| 4 | 118 | 0.71 | 0.92 | 21 | empty |
| 5 | 188 | 0.70 | 0.88 | 41 | empty |
Interfaces
12 interfaces between chains.
- A–B · 3341 Ų buried · 40 hydrogen bonds · protein-protein
- C–D · 3143 Ų buried · 38 hydrogen bonds · protein-protein
- D–H · 853 Ų buried · 25 hydrogen bonds · protein-protein
- A–E · 836 Ų buried · 23 hydrogen bonds · protein-protein
- B–F · 832 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 23 modified (engineered).
Compared structures
- 2AXZ · Crystal structure of PrgX/cCF10 complex · 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 Q04114
- Elsewhere: RCSB PDB 2AXZ · PDBe 2AXZ · UniProt Q04114
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