Research workbench
Solution NMR structure of CBM64 from S.THERMOPHILA using 20% 13C, 100% 15N
Analyse Solution NMR structure of CBM64 from S.THERMOPHILA using 20% 13C, 100% 15N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FFU
- Type
- protein
- Length
- 86 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl hydrolase family 5 cellulase CBM64
- UniProt
- E0RQU0
Structure
solution nmr · 1 distinct chain · 3% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyl hydrolase family 5 cellulase CBM64 | protein | 86 | 3% helix, 42% strand | E0RQU0 |
Compared structures
- 6FFU · Solution NMR structure of CBM64 from S.thermophila using 20% 13C, 100% 15N · 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 E0RQU0
- Elsewhere: RCSB PDB 6FFU · PDBe 6FFU · UniProt E0RQU0
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