Research workbench
H145Q mutant of mycobacterium tuberculosis iron-superoxide dismutase.
Analyse H145Q mutant of mycobacterium tuberculosis iron-superoxide dismutase. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GN3
- Type
- protein
- Length
- 396 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P17670
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 198 | — | P17670 |
Compared structures
- 1GN3 · H145Q mutant of Mycobacterium tuberculosis iron-superoxide dismutase. · 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 P17670
- Elsewhere: RCSB PDB 1GN3 · PDBe 1GN3 · UniProt P17670
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