Research workbench
AlphaFold monomer V2.0 prediction for peptidoglycan-recognition protein sd (Q9VS97)
Analyse AlphaFold monomer V2.0 prediction for peptidoglycan-recognition protein sd… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9VS97
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Peptidoglycan-recognition protein sd
- UniProt
- Q9VS97
Structure
1 distinct chain · 25% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan-recognition protein sd | protein | 186 | 25% helix, 18% strand | Q9VS97 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2RKQ · Crystal structure of drosophila peptidoglycan recognition protein SD (PGRP-SD) · an experimental structure of the same protein · chain A against A, TM-score 0.89
- 2RKQ · Crystal structure of drosophila peptidoglycan recognition protein sd (pgrp-sd) · an experimental structure of the same protein · chain A against A, TM-score 0.89
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 Q9VS97
- Elsewhere: UniProt Q9VS97 · AlphaFold DB Q9VS97
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