Research workbench
Structure of the caulobacter crescentus S-layer protein rsaa N- terminal domain bound to lps and soaked with holmium
Analyse Structure of the caulobacter crescentus S-layer protein rsaa N- terminal domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PEO
- Type
- protein
- Length
- 242 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-layer protein
- UniProt
- P35828
- Ligands
- MRH, BMA, CA, HO
- Pockets
- 4 · best druggability 0.43
Structure
electron microscopy · 1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-layer protein | protein | 242 | 67% helix, 1% strand | P35828 |
Ligands and binding sites
- MRH · 4-acetamido-4,6-dideoxy-alpha-D-mannopyranose · ligand · 8 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 4 copies · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- HO · Holmium atom · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.43 | 0.78 | 17 | empty |
| 2 | 66 | 0.29 | 0.73 | 13 | empty |
| 3 | 55 | 0.29 | 0.75 | 13 | MRH |
| 4 | 54 | 0.26 | 0.74 | 14 | empty |
Compared structures
- 7PEO · Structure of the Caulobacter crescentus S-layer protein RsaA N-terminal domain bound to… · the same entry in another collection · chain A against A, TM-score 1.00
- P35828 · AlphaFold monomer V2.0 prediction for S-layer protein (P35828) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P35828
- Elsewhere: RCSB PDB 7PEO · PDBe 7PEO · UniProt P35828
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