Research workbench
Mxih needle protein of shigella flexneri (monomeric form, residues 1-78)
Analyse Mxih needle protein of shigella flexneri (monomeric form, residues 1-78) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CA5
- Type
- protein
- Length
- 123 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mxih
- UniProt
- P0A223
- Ligands
- NA
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mxih | protein | 62 | 87% helix, 0% strand | P0A223 |
| B | Mxih | protein | 61 | 75% helix, 0% strand | P0A223 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
- IPA · Isopropyl alcohol · additive · 2 copies · chains A, B
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 95 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 P0A223
- Elsewhere: RCSB PDB 2CA5 · PDBe 2CA5 · UniProt P0A223
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