Research workbench
NMR structure and 1H, 13C and 15N chemical shift assignments for high mobility group protein from plasmodium falciparum 3D7.
Analyse NMR structure and 1H, 13C and 15N chemical shift assignments for high mobility… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MRC
- Type
- protein
- Length
- 92 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High mobility group protein
- UniProt
- Q8IB14
Structure
solution nmr · 1 distinct chain · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High mobility group protein | protein | 92 | 64% helix, 0% strand | Q8IB14 |
Compared structures
- 2MRC · NMR Structure and 1H, 13C and 15N Chemical Shift Assignments for High mobility group… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8IB14
- Elsewhere: RCSB PDB 2MRC · PDBe 2MRC · UniProt Q8IB14
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