Research workbench
Crystal structure of human B type phosphoglycerate mutase
Analyse Crystal structure of human B type phosphoglycerate mutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GPI
- Type
- protein
- Length
- 475 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglycerate mutase 1
- EC
- 3.1.3.13, 5.4.2.1, 5.4.2.4
- UniProt
- P18669
- Ligands
- CL
- Pockets
- 5 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Phosphoglycerate mutase 1 (EC 3.1.3.13, 5.4.2.1, 5.4.2.4) | protein | 240 | 47% helix, 12% strand | P18669 |
| C | Phosphoglycerate mutase 1 (EC 3.1.3.13, 5.4.2.1, 5.4.2.4) | protein | 235 | 43% helix, 14% strand | P18669 |
Ligands and binding sites
- CL · Chloride ion · ion · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.56 | 0.79 | 24 | empty |
| 2 | 230 | 0.56 | 0.78 | 31 | empty |
| 3 | 192 | 0.46 | 0.75 | 27 | empty |
| 4 | 156 | 0.43 | 0.74 | 20 | empty |
| 5 | 118 | 0.41 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- B–C · 1076 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
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 P18669
- Elsewhere: RCSB PDB 4GPI · PDBe 4GPI · UniProt P18669
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