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Crystal structure of C. albicans TRNA(HIS) guanylyltransferase (THG1) with a G-1 deleted TRNA(HIS)
Analyse Crystal structure of C. albicans TRNA(HIS) guanylyltransferase (THG1) with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WC1
- Type
- protein + RNA
- Length
- 1,098 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Likely histidyl tRNA-specific guanylyltransferase; 75-mer tRNA
- UniProt
- Q5AFK5
- Pockets
- 13 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Likely histidyl tRNA-specific guanylyltransferase | protein | 238 | 51% helix, 18% strand | Q5AFK5 |
| P, Q | 75-mer tRNA | rna | 73 | — | — |
Pockets
13 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 796 | 0.83 | 0.85 | 70 | empty |
| 2 | 679 | 0.80 | 0.85 | 68 | empty |
| 3 | 853 | 0.78 | 0.81 | 75 | empty |
| 4 | 1029 | 0.73 | 0.77 | 50 | empty |
| 5 | 892 | 0.71 | 0.76 | 47 | empty |
Interfaces
14 interfaces between chains.
- A–B · 2347 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 2347 Ų buried · 27 hydrogen bonds · protein-protein
- A–P · 603 Ų buried · 2 hydrogen bonds · protein-nucleic
- C–Q · 584 Ų buried · 13 hydrogen bonds · protein-nucleic
- D–P · 512 Ų buried · 18 hydrogen bonds · protein-nucleic
Compared structures
- 3WC1 · Crystal structure of C. albicans tRNA(His) guanylyltransferase (Thg1) with a G-1 deleted… · 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 Q5AFK5
- Elsewhere: RCSB PDB 3WC1 · PDBe 3WC1 · UniProt Q5AFK5
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