Research workbench
Solution structure of R. palustris csgh
Analyse Solution structure of R. palustris csgh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N59
- Type
- protein
- Length
- 101 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein csgh
- UniProt
- E6VF87
Structure
solution nmr · 1 distinct chain · 3% helix, 69% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein csgh | protein | 101 | 3% helix, 69% strand | E6VF87 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2N59 · Solution Structure of R. palustris CsgH · 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 E6VF87
- Elsewhere: RCSB PDB 2N59 · PDBe 2N59 · UniProt E6VF87
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