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Hypoxanthine phosphoribosyltransferase from E. COLI

Analyse Hypoxanthine phosphoribosyltransferase from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GRV
Type: protein
Length: 337 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypoxanthine phosphoribosyltransferase
EC: 2.4.2.8
UniProt: P36766
Ligands: MG
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8)	protein	168	26% helix, 35% strand	P36766
B	Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8)	protein	169	25% helix, 35% strand	P36766

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains B, A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	216	0.52	0.77	29	empty
2	223	0.48	0.74	30	empty
3	91	0.37	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 1288 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

1GRV · Hypoxanthine Phosphoribosyltransferase from E. coli · 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 P36766
Elsewhere: RCSB PDB 1GRV · PDBe 1GRV · UniProt P36766

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