Research workbench
Crystal structure of a SEC72-SSA1 C-terminal peptide fusion protein
Analyse Crystal structure of a SEC72-SSA1 C-terminal peptide fusion protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L0Y
- Type
- protein
- Length
- 1,203 residues
- Chains
- 13
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SEC72-SSA1 C-terminal peptide fusion protein; Pro-thr-val-glu-glu-val-asp
- UniProt
- G0SH41
- Pockets
- 10 · best druggability 0.72
Structure
x-ray diffraction · 11 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SEC72-SSA1 C-terminal peptide fusion protein | protein | 155 | 77% helix, 0% strand | G0SH41 |
| B | SEC72-SSA1 C-terminal peptide fusion protein | protein | 149 | 78% helix, 0% strand | G0SH41 |
| C | SEC72-SSA1 C-terminal peptide fusion protein | protein | 150 | 78% helix, 0% strand | G0SH41 |
| D | SEC72-SSA1 C-terminal peptide fusion protein | protein | 150 | 77% helix, 0% strand | G0SH41 |
| E | SEC72-SSA1 C-terminal peptide fusion protein | protein | 151 | 76% helix, 0% strand | G0SH41 |
| F | SEC72-SSA1 C-terminal peptide fusion protein | protein | 140 | 80% helix, 0% strand | G0SH41 |
| G | SEC72-SSA1 C-terminal peptide fusion protein | protein | 144 | 79% helix, 0% strand | G0SH41 |
| H | SEC72-SSA1 C-terminal peptide fusion protein | protein | 133 | 79% helix, 0% strand | G0SH41 |
| I, L | Pro-thr-val-glu-glu-val-asp | protein | 6 | 0% helix, 0% strand | — |
| J, K | Pro-thr-val-glu-glu-val-asp | protein | 7 | 43% helix, 0% strand | — |
| M | Pro-thr-val-glu-glu-val-asp | protein | 5 | 0% helix, 0% strand | — |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 973 | 0.72 | 0.76 | 73 | empty |
| 2 | 624 | 0.65 | 0.75 | 47 | empty |
| 3 | 111 | 0.54 | 0.83 | 27 | empty |
| 4 | 244 | 0.49 | 0.74 | 44 | empty |
| 5 | 246 | 0.48 | 0.74 | 35 | empty |
Interfaces
17 interfaces between chains.
- A–F · 808 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 686 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 674 Ų buried · 17 hydrogen bonds · protein-protein
- E–H · 520 Ų buried · 15 hydrogen bonds · protein-protein
- F–J · 510 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5L0Y · Crystal Structure of a Sec72-ssa1 c-terminal peptide fusion protein · 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 G0SH41
- Elsewhere: RCSB PDB 5L0Y · PDBe 5L0Y · UniProt G0SH41
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