Research workbench
Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase mgp complexed with man-GLC+PO4
Analyse Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase mgp complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WAS
- Type
- protein
- Length
- 778 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5LH68
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 389 | — | Q5LH68 |
Compared structures
- 3WAS · Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with… · the same entry in another collection · chain B against B, TM-score 1.00
- Q5LH68 · AlphaFold monomer V2.0 prediction for 4-O-beta-D-mannosyl-D-glucose phosphorylase (Q5LH68) · a predicted model of the same protein · 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 Q5LH68
- Elsewhere: RCSB PDB 3WAS · PDBe 3WAS · UniProt Q5LH68
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