MolNFT v1 · #168663 · protein
Crystal structure of an aspartate ammonia-lyase from elizabethkingia anophelis NUHP1
6WNG: “Crystal structure of an aspartate ammonia-lyase from elizabethkingia anophelis NUHP1”. X-ray diffraction, 2 ligands (FUM, CL). MolNFT v1 #168663 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6WNG
- Type
- protein
- Length
- 1,864 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- X5KSV5
- Ligands
- FUM, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 466 | — | X5KSV5 |
Ligands and binding sites
- FUM · Fumaric acid · ligand · 4 copies · chains A, B, D, C
- CL · Chloride ion · ion · 12 copies · chains A, C, D, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 4 copies · chains A, D, B, C
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6WNG · Crystal structure of an aspartate ammonia-lyase from Elizabethkingia anophelis NUHP1 · 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 X5KSV5
- Elsewhere: RCSB PDB 6WNG · PDBe 6WNG · UniProt X5KSV5
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