Research workbench
Human impase with mn
Analyse Human impase with mn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GJ0
- Type
- protein
- Length
- 549 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inositol monophosphatase 1
- EC
- 3.1.3.25, 3.1.3.94
- UniProt
- P29218
- Ligands
- MN
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inositol monophosphatase 1 (EC 3.1.3.25, 3.1.3.94) | protein | 274 | 37% helix, 24% strand | P29218 |
| B | Inositol monophosphatase 1 (EC 3.1.3.25, 3.1.3.94) | protein | 275 | 36% helix, 25% strand | P29218 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 6 copies · chains A, B
- GOL · Glycerol · additive · 6 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 404 | 0.77 | 0.86 | 47 | MN, GOL, MES |
| 2 | 390 | 0.76 | 0.86 | 52 | MN, GOL, MES |
| 3 | 474 | 0.62 | 0.75 | 57 | GOL |
| 4 | 103 | 0.36 | 0.74 | 17 | empty |
| 5 | 77 | 0.34 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1661 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P29218
- Elsewhere: RCSB PDB 6GJ0 · PDBe 6GJ0 · UniProt P29218
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