Research workbench
X-ray structure of the unliganded uridine phosphorylase from vibrio cholerae at 1.22A
Analyse X-ray structure of the unliganded uridine phosphorylase from vibrio cholerae at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EYP
- Type
- protein
- Length
- 1,508 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9K4U1
- Ligands
- NA, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, E | — | protein | 251 | — | Q9K4U1 |
| B, F | — | protein | 252 | — | Q9K4U1 |
Ligands and binding sites
- NA · Sodium ion · metal · 3 copies · chains A, B, C, D, E, F
- MG · Magnesium ion · metal · chains C
- GOL · Glycerol · additive · 8 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6EYP · X-ray structure of the unliganded uridine phosphorylase from Vibrio cholerae at 1.22A · 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 Q9K4U1
- Elsewhere: RCSB PDB 6EYP · PDBe 6EYP · UniProt Q9K4U1
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