PDBsum entry 2q7o

Transferase

PDB id: 2q7o

Contents

Protein chain

284 a.a. *

Ligands

PO4

IMH

Waters ×21

* Residue conservation analysis

PDB id:

2q7o

Name:

Transferase

Title:

Structure of human purine nucleoside phosphorylase in complex with l- immucillin-h

Structure:

Purine nucleoside phosphorylase. Chain: e. Synonym: inosine phosphorylase, pnp. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: np, pnp. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.90Å R-factor: 0.218 R-free: 0.262

Authors:

A.Rinaldo-Matthis,S.C.Almo,V.L.Schramm

Key ref:

A.Rinaldo-Matthis et al. (2008). L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase. J Am Chem Soc, 130, 842-844. PubMed id: 18154341

Date:

07-Jun-07 Release date: 15-Jan-08

Protein chain

P00491  (PNPH_HUMAN) -  Purine nucleoside phosphorylase from Homo sapiens

Seq: 289 a.a.

Struc: 284 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.4.2.1 - purine-nucleoside phosphorylase.
• Reaction:
  1. a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha- D-ribose 1-phosphate
  2. a purine 2'-deoxy-D-ribonucleoside + phosphate = a purine nucleobase + 2-deoxy-alpha-D-ribose 1-phosphate

purine D-ribonucleoside + phosphate (Bound ligand (Het Group name = PO4) corresponds exactly) = purine nucleobase + alpha- D-ribose 1-phosphate

purine 2'-deoxy-D-ribonucleoside + phosphate (Bound ligand (Het Group name = PO4) corresponds exactly) = purine nucleobase + 2-deoxy-alpha-D-ribose 1-phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

J Am Chem Soc 130:842-844 (2008)

PubMed id: 18154341

L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase.

A.Rinaldo-Matthis, A.S.Murkin, U.A.Ramagopal, K.Clinch, S.P.Mee, G.B.Evans, P.C.Tyler, R.H.Furneaux, S.C.Almo, V.L.Schramm.

ABSTRACT

Human purine nucleoside phosphorylase (PNP) was crystallized with transition-state analogue inhibitors Immucillin-H and DADMe-Immucillin-H synthesized with ribosyl mimics of l-stereochemistry. The inhibitors demonstrate that major driving forces for tight binding of these analogues are the leaving group interaction and the cationic mimicry of the transition state, even though large geometric changes occur with d-Immucillins and l-Immucillins bound to human PNP.