Research workbench
1H, 13C, and 15N chemical shift assignments for in-cell GB1
Analyse 1H, 13C, and 15N chemical shift assignments for in-cell GB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N9L
- Type
- protein
- Length
- 57 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin G-binding protein G
- UniProt
- P19909
Structure
solution nmr · 1 distinct chain · 26% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Immunoglobulin G-binding protein G | protein | 57 | 26% helix, 46% strand | P19909 |
Compared structures
- 2N9L · 1H, 13C, and 15N Chemical Shift Assignments for in-cell GB1 · the same entry in another collection · chain A against A, TM-score 1.00
- P19909 · AlphaFold monomer V2.0 prediction for immunoglobulin G-binding protein G (P19909) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P19909
- Elsewhere: RCSB PDB 2N9L · PDBe 2N9L · UniProt P19909
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