Research workbench
Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
Analyse Crystal structure of gmp synthetase from thermus thermophilus 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
- 2YWC
- Type
- protein
- Length
- 1,876 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5SI28
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 475 | — | Q5SI28 |
| B, C | — | protein | 467 | — | Q5SI28 |
| D | — | protein | 467 | — | Q5SI28 |
Compared structures
- 2YWC · Crystal structure of GMP synthetase from Thermus thermophilus in complex with XMP · the same entry in another collection · chain A against A, TM-score 1.00
- Q5SI28 · AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] (Q5SI28) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q5SI28
- Elsewhere: RCSB PDB 2YWC · PDBe 2YWC · UniProt Q5SI28
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