Research workbench
Crystal structure of SLY1P in complex with an N-terminal peptide of SED5P
Analyse Crystal structure of SLY1P in complex with an N-terminal peptide of SED5P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MQS
- Type
- protein
- Length
- 614 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SLY1 protein; Integral membrane protein SED5
- UniProt
- P22213, Q01590
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SLY1 protein | protein | 588 | 49% helix, 13% strand | P22213 |
| B | Integral membrane protein SED5 | protein | 26 | 73% helix, 4% strand | Q01590 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1184 | 0.78 | 0.80 | 126 | empty |
| 2 | 141 | 0.45 | 0.76 | 20 | empty |
| 3 | 125 | 0.45 | 0.78 | 28 | empty |
| 4 | 102 | 0.35 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1085 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 1MQS · Crystal structure of Sly1p in complex with an N-terminal peptide of Sed5p · the same entry in another collection · chain A against A, TM-score 1.00
- P22213 · AlphaFold monomer V2.0 prediction for protein SLY1 (P22213) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q01590 · AlphaFold monomer V2.0 prediction for integral membrane protein SED5 (Q01590) · a predicted model of the same protein · chain B against A, TM-score 0.59
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 P22213
- Every structure of UniProt Q01590
- Elsewhere: RCSB PDB 1MQS · PDBe 1MQS · UniProt P22213 · UniProt Q01590
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