This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1w2d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 1w2d |SIZE=350|CAPTION= <scene name='initialview01'>1w2d</scene>, resolution 1.94&Aring;
|PDB= 1w2d |SIZE=350|CAPTION= <scene name='initialview01'>1w2d</scene>, resolution 1.94&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
-
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>
+
|LIGAND= <scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.7.127 2.1.7.127]
+
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.7.127 2.1.7.127] </span>
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w2d OCA], [http://www.ebi.ac.uk/pdbsum/1w2d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w2d RCSB]</span>
}}
}}
Line 27: Line 30:
[[Category: Schell, M J.]]
[[Category: Schell, M J.]]
[[Category: Williams, R L.]]
[[Category: Williams, R L.]]
-
[[Category: 4IP]]
 
-
[[Category: ADP]]
 
-
[[Category: MN]]
 
-
[[Category: SO4]]
 
[[Category: adp]]
[[Category: adp]]
[[Category: inositol phosphate kinase]]
[[Category: inositol phosphate kinase]]
Line 36: Line 35:
[[Category: transferase]]
[[Category: transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:03:26 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:14 2008''

Revision as of 21:30, 30 March 2008


PDB ID 1w2d

Drag the structure with the mouse to rotate
, resolution 1.94Å
Sites:
Ligands: , , ,
Activity: Transferase, with EC number 2.1.7.127
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



HUMAN INOSITOL (1,4,5)-TRISPHOSPHATE 3-KINASE COMPLEXED WITH MN2+/ADP/INS(1,3,4,5)P4


Overview

Mammalian cells produce a variety of inositol phosphates (InsPs), including Ins(1,4,5)P3 that serves both as a second messenger and as a substrate for inositol polyphosphate kinases (IPKs), which further phosphorylate it. We report the structure of an IPK, the human Ins(1,4,5)P3 3-kinase-A, both free and in complexes with substrates and products. This enzyme catalyzes transfer of a phosphate from ATP to the 3-OH of Ins(1,4,5)P3, and its X-ray crystal structure provides a template for understanding a broad family of InsP kinases. The catalytic domain consists of three lobes. The N and C lobes bind ATP and resemble protein and lipid kinases, despite insignificant sequence similarity. The third lobe binds inositol phosphate and is a unique four-helix insertion in the C lobe. This lobe embraces all of the phosphates of Ins(1,4,5)P3 in a positively charged pocket, explaining the enzyme's substrate specificity and its inability to phosphorylate PtdIns(4,5)P2, the membrane-resident analog of Ins(1,4,5)P3.

About this Structure

1W2D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase., Gonzalez B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL, Mol Cell. 2004 Sep 10;15(5):689-701. PMID:15350214

Page seeded by OCA on Mon Mar 31 00:30:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools