Research workbench
Crystal structure of human hisrs
Analyse Crystal structure of human hisrs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G84
- Type
- protein
- Length
- 871 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine--tRNA ligase, cytoplasmic
- EC
- 6.1.1.21
- UniProt
- P12081
- Ligands
- CL
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine--tRNA ligase, cytoplasmic (EC 6.1.1.21) | protein | 433 | 44% helix, 21% strand | P12081 |
| B | Histidine--tRNA ligase, cytoplasmic (EC 6.1.1.21) | protein | 438 | 45% helix, 20% strand | P12081 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 716 | 0.80 | 0.84 | 45 | empty |
| 2 | 403 | 0.65 | 0.79 | 39 | IMD |
| 3 | 376 | 0.60 | 0.77 | 35 | IMD |
| 4 | 212 | 0.55 | 0.78 | 24 | empty |
| 5 | 206 | 0.54 | 0.78 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 4310 Ų buried · 58 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 P12081
- Elsewhere: RCSB PDB 4G84 · PDBe 4G84 · UniProt P12081
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