Research workbench
Crystal structure of saccharomyces cerevisiae DCP2 nudix domain in complex with mg (E153Q mutation)
Analyse Crystal structure of saccharomyces cerevisiae DCP2 nudix domain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KG3
- Type
- protein
- Length
- 427 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53550
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 138 | — | P53550 |
| B | — | protein | 145 | — | P53550 |
| C | — | protein | 144 | — | P53550 |
Compared structures
- 4KG3 · Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain in complex with Mg (E153Q… · the same entry in another collection · chain A against A, TM-score 1.00
- P53550 · AlphaFold monomer V2.0 prediction for M7GPPPN-mRNA hydrolase (P53550) · a predicted model of the same protein · chain A 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 P53550
- Elsewhere: RCSB PDB 4KG3 · PDBe 4KG3 · UniProt P53550
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