MolNFT v1 · #38654 · protein
Human bisphosphoglycerate mutase complexed with 2,3- bisphosphoglycerate
2H4Z: “Human bisphosphoglycerate mutase complexed with 2,3- bisphosphoglycerate”. X-ray diffraction, 1 ligand (DG2), 7 pockets (best druggability 0.78). MolNFT v1 #38654 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2H4Z
- Type
- protein
- Length
- 509 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bisphosphoglycerate mutase
- EC
- 5.4.2.4, 5.4.2.1, 3.1.3.13
- UniProt
- P07738
- Ligands
- DG2
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bisphosphoglycerate mutase (EC 5.4.2.4, 5.4.2.1, 3.1.3.13) | protein | 255 | 46% helix, 12% strand | P07738 |
| B | Bisphosphoglycerate mutase (EC 5.4.2.4, 5.4.2.1, 3.1.3.13) | protein | 254 | 45% helix, 12% strand | P07738 |
Ligands and binding sites
- DG2 · (2R)-2,3-diphosphoglyceric acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.78 | 0.96 | 28 | DG2 |
| 2 | 105 | 0.75 | 0.96 | 30 | DG2 |
| 3 | 394 | 0.62 | 0.77 | 56 | empty |
| 4 | 150 | 0.52 | 0.79 | 19 | empty |
| 5 | 67 | 0.39 | 0.80 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 956 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 2H4Z · Human bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerate · 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 2H4Z · PDBe 2H4Z · UniProt P07738
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