Research workbench
The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound gmp
Analyse The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HMP
- Type
- protein
- Length
- 423 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypoxanthine guanine phosphoribosyl-transferase
- EC
- 2.4.2.8
- UniProt
- P00492
- Ligands
- 5GP
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypoxanthine guanine phosphoribosyl-transferase (EC 2.4.2.8) | protein | 214 | 28% helix, 28% strand | P00492 |
| B | Hypoxanthine guanine phosphoribosyl-transferase (EC 2.4.2.8) | protein | 209 | 26% helix, 28% strand | P00492 |
Ligands and binding sites
- 5GP · Guanosine-5'-monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 749 | 0.71 | 0.77 | 82 | 5GP |
| 2 | 161 | 0.48 | 0.77 | 32 | empty |
| 3 | 121 | 0.41 | 0.76 | 19 | 5GP |
Interfaces
1 interface between chains.
- A–B · 1468 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 1HMP · The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound… · the same entry in another collection · chain A against A, TM-score 1.00
- P00492 · AlphaFold monomer V2.0 prediction for hypoxanthine-guanine phosphoribosyltransferase… · a predicted model of the same protein · chain B against A, TM-score 0.91
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 P00492
- Elsewhere: RCSB PDB 1HMP · PDBe 1HMP · UniProt P00492
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