Research workbench
INLB392_T332E: T332E variant of listeria monocytogenes inlb (internalin B) residues 36-392
Analyse INLB392_T332E: T332E variant of listeria monocytogenes inlb (internalin B)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NMS
- Type
- protein
- Length
- 357 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Internalin B
- UniProt
- P0DQD2
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Internalin B | protein | 357 | 13% helix, 33% strand | P0DQD2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NMS · InlB392_T332E: T332E variant of Listeria monocytogenes InlB (internalin B) residues 36-392 · the same entry in another collection · chain A against A, TM-score 1.00
- P0DQD2 · AlphaFold monomer V2.0 prediction for internalin B (P0DQD2) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P0DQD2
- Elsewhere: RCSB PDB 7NMS · PDBe 7NMS · UniProt P0DQD2
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