Research workbench
Crystal structure of neisseria meningitidis nada variant 3 double mutant A33I-I38L
Analyse Crystal structure of neisseria meningitidis nada variant 3 double mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EUP
- Type
- protein
- Length
- 441 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8KH85
- Ligands
- PO4, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 147 | — | Q8KH85 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains B, C, A
- CL · Chloride ion · ion · chains A, B, C
- EDO · 1,2-ethanediol · additive · 18 copies · chains A, B, C
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 5 copies · chains A, C, B
- P6G · Hexaethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6EUP · Crystal structure of Neisseria meningitidis NadA variant 3 double mutant A33I-I38L · 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 Q8KH85
- Elsewhere: RCSB PDB 6EUP · PDBe 6EUP · UniProt Q8KH85
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