Research workbench
Crystal structure of human apo-qprt
Analyse Crystal structure of human apo-qprt in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KWV
- Type
- protein
- Length
- 1,720 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- EC
- 2.4.2.19
- UniProt
- Q15274
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) | protein | 285 | 45% helix, 19% strand | Q15274 |
| B | Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) | protein | 286 | 45% helix, 19% strand | Q15274 |
| E | Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) | protein | 288 | 45% helix, 19% strand | Q15274 |
| F | Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) | protein | 291 | 44% helix, 20% strand | Q15274 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 745 | 0.85 | 0.89 | 107 | empty |
| 2 | 608 | 0.79 | 0.85 | 58 | empty |
| 3 | 665 | 0.79 | 0.84 | 62 | empty |
| 4 | 537 | 0.78 | 0.85 | 59 | empty |
| 5 | 498 | 0.78 | 0.85 | 54 | empty |
Interfaces
15 interfaces between chains.
- E–F · 2341 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 2295 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 2286 Ų buried · 33 hydrogen bonds · protein-protein
- B–E · 673 Ų buried · 2 hydrogen bonds · protein-protein
- C–E · 671 Ų buried · 2 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 Q15274
- Elsewhere: RCSB PDB 4KWV · PDBe 4KWV · UniProt Q15274
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.