Research workbench
Crystal structure of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, in the substrate complex
Analyse Crystal structure of N-acetylglucosamine-phosphate mutase, a member of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DKC
- Type
- protein
- Length
- 1,071 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9P4V2
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 536 | — | Q9P4V2 |
| B | — | protein | 535 | — | Q9P4V2 |
Compared structures
- 2DKC · Crystal structure of N-acetylglucosamine-phosphate mutase, a member of the… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9P4V2 · AlphaFold monomer V2.0 prediction for phosphoacetylglucosamine mutase (Q9P4V2) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9P4V2
- Elsewhere: RCSB PDB 2DKC · PDBe 2DKC · UniProt Q9P4V2
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