3bgs

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|PDB= 3bgs |SIZE=350|CAPTION= <scene name='initialview01'>3bgs</scene>, resolution 2.099&Aring;
|PDB= 3bgs |SIZE=350|CAPTION= <scene name='initialview01'>3bgs</scene>, resolution 2.099&Aring;
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Residue+A+302'>AC1</scene>, <scene name='pdbsite=AC2:Po4+Binding+Site+For+Residue+A+303'>AC2</scene>, <scene name='pdbsite=AC3:Po4+Binding+Site+For+Residue+A+304'>AC3</scene> and <scene name='pdbsite=AC4:Dih+Binding+Site+For+Residue+A+301'>AC4</scene>
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Residue+A+302'>AC1</scene>, <scene name='pdbsite=AC2:Po4+Binding+Site+For+Residue+A+303'>AC2</scene>, <scene name='pdbsite=AC3:Po4+Binding+Site+For+Residue+A+304'>AC3</scene> and <scene name='pdbsite=AC4:Dih+Binding+Site+For+Residue+A+301'>AC4</scene>
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=DIH:3-HYDROXY-4-HYDROXYMETHYL-1-(4-OXO-4,4A,5,7A-TETRAHYDRO-3H-PYRROLO[3,2-D]PYRIMIDIN-7-YLMETHYL)-PYRROLIDINIUM'>DIH</scene>
+
|LIGAND= <scene name='pdbligand=DIH:3-HYDROXY-4-HYDROXYMETHYL-1-(4-OXO-4,4A,5,7A-TETRAHYDRO-3H-PYRROLO[3,2-D]PYRIMIDIN-7-YLMETHYL)-PYRROLIDINIUM'>DIH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] </span>
|GENE= NP, PNP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= NP, PNP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
|DOMAIN=
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|RELATEDENTRY=[[1rr6|1RR6]], [[1rt9|1RT9]], [[1rsz|1RSZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bgs OCA], [http://www.ebi.ac.uk/pdbsum/3bgs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bgs RCSB]</span>
}}
}}
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[[Category: Ramagopal, U A.]]
[[Category: Ramagopal, U A.]]
[[Category: Schramm, V L.]]
[[Category: Schramm, V L.]]
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[[Category: DIH]]
 
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[[Category: PO4]]
 
[[Category: l-enantiomer]]
[[Category: l-enantiomer]]
[[Category: pnp]]
[[Category: pnp]]
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[[Category: transition state analogue]]
[[Category: transition state analogue]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:58:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:26:07 2008''

Revision as of 02:26, 31 March 2008


PDB ID 3bgs

Drag the structure with the mouse to rotate
, resolution 2.099Å
Sites: , , and
Ligands: ,
Gene: NP, PNP (Homo sapiens)
Activity: Purine-nucleoside phosphorylase, with EC number 2.4.2.1
Related: 1RR6, 1RT9, 1RSZ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of human purine nucleoside phosphorylase with L-DADMe-ImmH and phosphate


Overview

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.

About this Structure

3BGS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase., Rinaldo-Matthis A, Murkin AS, Ramagopal UA, Clinch K, Mee SP, Evans GB, Tyler PC, Furneaux RH, Almo SC, Schramm VL, J Am Chem Soc. 2008 Jan 23;130(3):842-4. Epub 2007 Dec 23. PMID:18154341

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