Research workbench
Solution NMR structure of a putative thioredoxin (ECH_0218) in the oxidized state from ehrlichia chaffeensis, the etiological agent responsible for human monocytic ehrlichiosis. seattle structural genomics center for infectious disease target EHCHA.00546.A
Analyse Solution NMR structure of a putative thioredoxin (ECH_0218) in the oxidized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ALI
- Type
- protein
- Length
- 128 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2GHP2
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 128 | — | Q2GHP2 |
Compared structures
- 6ALI · Solution NMR structure of a putative thioredoxin (ECH_0218) in the oxidized state from… · 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 Q2GHP2
- Elsewhere: RCSB PDB 6ALI · PDBe 6ALI · UniProt Q2GHP2
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