Research workbench
Crystal structure of histidine--tRNA ligase from elizabethkingia sp. ccug 26117
Analyse Crystal structure of histidine--tRNA ligase from elizabethkingia sp. ccug 26117 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NHI
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine--tRNA ligase
- EC
- 6.1.1.21
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine--tRNA ligase (EC 6.1.1.21) | protein | 448 | 44% helix, 19% strand | — |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 505 | 0.63 | 0.76 | 52 | empty |
| 2 | 151 | 0.46 | 0.76 | 21 | empty |
| 3 | 73 | 0.43 | 0.80 | 16 | empty |
Compared structures
- 6NHI · Crystal structure of Histidine--tRNA ligase from Elizabethkingia sp. CCUG 26117 · 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
- Elsewhere: RCSB PDB 6NHI · PDBe 6NHI
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