MolNFT v1 · #146173 · protein
The sulfate-bound crystal structure of hprt (hypoxanthine phosphoribosyltransferase)
6D9Q: “The sulfate-bound crystal structure of hprt (hypoxanthine phosphoribosyltransferase)”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.63). MolNFT v1 #146173 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6D9Q
- Type
- protein
- Length
- 722 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypoxanthine phosphoribosyltransferase
- EC
- 2.4.2.8
- UniProt
- A0A1S0QLD4
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) | protein | 181 | 31% helix, 31% strand | A0A1S0QLD4 |
| B, D | Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) | protein | 180 | 28% helix, 32% strand | A0A1S0QLD4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 479 | 0.63 | 0.76 | 39 | SO4 |
| 2 | 443 | 0.62 | 0.76 | 36 | SO4 |
| 3 | 458 | 0.62 | 0.76 | 38 | SO4 |
| 4 | 425 | 0.61 | 0.76 | 40 | SO4 |
Interfaces
6 interfaces between chains.
- A–C · 1798 Ų buried · 25 hydrogen bonds · protein-protein
- B–D · 1777 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 937 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 930 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 74 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6D9Q · The sulfate-bound crystal structure of HPRT (hypoxanthine phosphoribosyltransferase) · 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 A0A1S0QLD4
- Elsewhere: RCSB PDB 6D9Q · PDBe 6D9Q · UniProt A0A1S0QLD4
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