Research workbench
Crystal structure of the putative histidinol phosphatase hisk from listeria monocytogenes. northeast structural genomics consortium target LMR141.
Analyse Crystal structure of the putative histidinol phosphatase hisk from listeria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DCP
- Type
- protein
- Length
- 821 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidinol-phosphatase
- EC
- 3.1.3.15
- UniProt
- Q4EIC3
- Ligands
- FE, ZN
- Pockets
- 8 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphatase (EC 3.1.3.15) | protein | 277 | 47% helix, 17% strand | Q4EIC3 |
| B | Histidinol-phosphatase (EC 3.1.3.15) | protein | 272 | 44% helix, 18% strand | Q4EIC3 |
| C | Histidinol-phosphatase (EC 3.1.3.15) | protein | 272 | 45% helix, 18% strand | Q4EIC3 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 6 copies · chains A, B, C
- ZN · Zinc ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 617 | 0.69 | 0.78 | 74 | ZN |
| 2 | 187 | 0.61 | 0.83 | 27 | FE |
| 3 | 264 | 0.60 | 0.80 | 32 | FE |
| 4 | 261 | 0.55 | 0.77 | 33 | empty |
| 5 | 65 | 0.45 | 0.83 | 23 | empty |
Interfaces
2 interfaces between chains.
- A–C · 486 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 331 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 23 modified (engineered).
Compared structures
- 3DCP · Crystal structure of the putative histidinol phosphatase hisK from Listeria… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q4EIC3
- Elsewhere: RCSB PDB 3DCP · PDBe 3DCP · UniProt Q4EIC3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.