1BZY
HUMAN HGPRTASE WITH TRANSITION STATE INHIBITOR
Summary for 1BZY
| Entry DOI | 10.2210/pdb1bzy/pdb |
| Descriptor | HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE, MAGNESIUM ION, PHOSPHORIC ACID MONO-[5-(2-AMINO-4-OXO-4,5-DIHYDRO-3H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)-3,4-DIHYDROXY-PYRROLIDIN-2-YLMETHYL] ESTER, ... (5 entities in total) |
| Functional Keywords | phosphoribosyltransferase, immucillin, lesch-nyhan, hgprt, transition state, magnesium, pyrophosphate, oxocarbenium ion, neighboring group participation |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P00492 |
| Total number of polymer chains | 4 |
| Total formula weight | 100268.14 |
| Authors | Shi, W.,Li, C.,Tyler, P.C.,Furneaux, R.H.,Grubmeyer, C.,Schramm, V.L.,Almo, S.C. (deposition date: 1998-11-05, release date: 1999-06-22, Last modification date: 2024-05-22) |
| Primary citation | Shi, W.,Li, C.M.,Tyler, P.C.,Furneaux, R.H.,Grubmeyer, C.,Schramm, V.L.,Almo, S.C. The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat.Struct.Biol., 6:588-593, 1999 Cited by PubMed Abstract: The structure of human HGPRT bound to the transition-state analog immucillinGP and Mg2+-pyrophosphate has been determined to 2.0 A resolution. ImmucillinGP was designed as a stable analog with the stereoelectronic features of the transition state. Bound inhibitor at the catalytic site indicates that the oxocarbenium ion of the transition state is stabilized by neighboring-group participation from MgPPi and O5'. A short hydrogen bond forms between Asp 137 and the purine ring analog. Two Mg2+ ions sandwich the pyrophosphate and contact both hydroxyls of the ribosyl analog. The transition-state analog is shielded from bulk solvent by a catalytic loop that moves approximately 25 A to cover the active site and becomes an ordered antiparallel beta-sheet. PubMed: 10360366DOI: 10.1038/9376 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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