Research workbench
Human bisphosphoglycerate mutase complex with 2-phosphoglycolate
Analyse Human bisphosphoglycerate mutase complex with 2-phosphoglycolate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N3S
- Type
- protein
- Length
- 497 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bisphosphoglycerate mutase
- EC
- 5.4.2.4, 5.4.2.11
- UniProt
- P07738
- Ligands
- PGA
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bisphosphoglycerate mutase (EC 5.4.2.4, 5.4.2.11) | protein | 254 | 46% helix, 12% strand | P07738 |
| B | Bisphosphoglycerate mutase (EC 5.4.2.4, 5.4.2.11) | protein | 243 | 41% helix, 12% strand | P07738 |
Ligands and binding sites
- PGA · 2-phosphoglycolic acid · ligand · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 400 | 0.65 | 0.79 | 44 | PGA |
| 2 | 435 | 0.65 | 0.78 | 49 | empty |
| 3 | 149 | 0.62 | 0.85 | 40 | PGA |
| 4 | 118 | 0.55 | 0.83 | 12 | PGA |
| 5 | 58 | 0.26 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 955 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7N3S · Human bisphosphoglycerate mutase complex with 2-phosphoglycolate · the same entry in another collection · chain A against A, TM-score 1.00
- P07738 · AlphaFold monomer V2.0 prediction for bisphosphoglycerate mutase (P07738) · 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 P07738
- Elsewhere: RCSB PDB 7N3S · PDBe 7N3S · UniProt P07738
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