MolNFT v1 · #83234 · protein
Crystal structure of C. albicans TRNA(HIS) guanylyltransferase (THG1) with ATP
3WBZ · Likely histidyl tRNA-specific guanylyltransferase: “Crystal structure of C. albicans TRNA(HIS) guanylyltransferase (THG1) with ATP”. X-ray diffraction, 2 ligands (ATP, MG), 20 pockets (best druggability 0.82). MolNFT v1 #83234 on…
- PDB
- 3WBZ
- Type
- protein
- Length
- 2,043 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Likely histidyl tRNA-specific guanylyltransferase
- EC
- 2.7.7.79
- UniProt
- Q5AFK5
- Ligands
- ATP, MG
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 7 distinct chains · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Likely histidyl tRNA-specific guanylyltransferase (EC 2.7.7.79) | protein | 244 | 50% helix, 17% strand | Q5AFK5 |
| B, G | Likely histidyl tRNA-specific guanylyltransferase (EC 2.7.7.79) | protein | 243 | 51% helix, 17% strand | Q5AFK5 |
| C | Likely histidyl tRNA-specific guanylyltransferase (EC 2.7.7.79) | protein | 265 | 51% helix, 16% strand | Q5AFK5 |
| D | Likely histidyl tRNA-specific guanylyltransferase (EC 2.7.7.79) | protein | 266 | 51% helix, 16% strand | Q5AFK5 |
| E | Likely histidyl tRNA-specific guanylyltransferase (EC 2.7.7.79) | protein | 268 | 50% helix, 16% strand | Q5AFK5 |
| F | Likely histidyl tRNA-specific guanylyltransferase (EC 2.7.7.79) | protein | 255 | 51% helix, 16% strand | Q5AFK5 |
| H | Likely histidyl tRNA-specific guanylyltransferase (EC 2.7.7.79) | protein | 259 | 51% helix, 16% strand | Q5AFK5 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 16 copies · chains A, B, E, C, D, F, G, H
- MG · Magnesium ion · metal · 24 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 893 | 0.82 | 0.84 | 95 | empty |
| 2 | 757 | 0.82 | 0.85 | 75 | empty |
| 3 | 1124 | 0.78 | 0.80 | 98 | ATP, MG |
| 4 | 1053 | 0.76 | 0.78 | 85 | ATP, MG |
| 5 | 321 | 0.70 | 0.84 | 52 | ATP, MG |
Interfaces
16 interfaces between chains.
- E–F · 2362 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 2318 Ų buried · 34 hydrogen bonds · protein-protein
- A–B · 2290 Ų buried · 34 hydrogen bonds · protein-protein
- G–H · 2267 Ų buried · 32 hydrogen bonds · protein-protein
- B–E · 683 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3WBZ · Crystal structure of C. albicans tRNA(His) guanylyltransferase (Thg1) with ATP · 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 3WBZ · PDBe 3WBZ · UniProt Q5AFK5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.