Research workbench
The structure of glucose-6-phosphate isomerase (gpi) from brucella melitensis
Analyse The structure of glucose-6-phosphate isomerase (gpi) from brucella melitensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EM6
- Type
- protein
- Length
- 2,182 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8YF86
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, A, B | — | protein | 546 | — | Q8YF86 |
| C | — | protein | 544 | — | Q8YF86 |
Compared structures
- 4EM6 · The structure of Glucose-6-phosphate isomerase (GPI) from Brucella melitensis · the same entry in another collection · chain C against C, TM-score 1.00
- Q8YF86 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase (Q8YF86) · a predicted model of the same protein · chain D 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 Q8YF86
- Elsewhere: RCSB PDB 4EM6 · PDBe 4EM6 · UniProt Q8YF86
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