Research workbench
Crystal structure of a phosphoglycerate mutase gpma from borrelia burgdorferi B31
Analyse Crystal structure of a phosphoglycerate mutase gpma from borrelia burgdorferi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EMB
- Type
- protein
- Length
- 971 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O51602
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 245 | — | O51602 |
| B, D | — | protein | 241 | — | O51602 |
| C | — | protein | 244 | — | O51602 |
Compared structures
- 4EMB · Crystal structure of a phosphoglycerate mutase gpmA from Borrelia burgdorferi B31 · the same entry in another collection · chain A against A, TM-score 1.00
- O51602 · AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- dependent phosphoglycerate… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O51602
- Elsewhere: RCSB PDB 4EMB · PDBe 4EMB · UniProt O51602
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