Research workbench
E. COLI pure H45Q mutant complexed with nitro-air
Analyse E. COLI pure H45Q mutant complexed with nitro-air in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NSH
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosylaminoimidazole carboxylase catalytic subunit
- EC
- 4.1.1.21
- UniProt
- P0AG18
- Ligands
- NIA
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylaminoimidazole carboxylase catalytic subunit (EC 4.1.1.21) | protein | 163 | 48% helix, 15% strand | P0AG18 |
Ligands and binding sites
- NIA · ((2R,3S,4R,5R)-5-(5-amino-4-nitro-1H-imidazol-1-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl dihydrogen phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P0AG18
- Elsewhere: RCSB PDB 2NSH · PDBe 2NSH · UniProt P0AG18
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