Research workbench
Pyridine nucleotide complexes with bacillus anthracis coenzyme a- disulfide reductase: a structural analysis of dual NAD(P)H specificity
Analyse Pyridine nucleotide complexes with bacillus anthracis coenzyme a- disulfide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CGB
- Type
- protein
- Length
- 888 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q81TK8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 444 | — | Q81TK8 |
Compared structures
- 3CGB · Pyridine Nucleotide Complexes with Bacillus anthracis Coenzyme A-Disulfide Reductase: A… · 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 Q81TK8
- Elsewhere: RCSB PDB 3CGB · PDBe 3CGB · UniProt Q81TK8
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