2hw4
From Proteopedia
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|PDB= 2hw4 |SIZE=350|CAPTION= <scene name='initialview01'>2hw4</scene>, resolution 1.90Å | |PDB= 2hw4 |SIZE=350|CAPTION= <scene name='initialview01'>2hw4</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene> | + | |LIGAND= <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= PHPT1, PHP14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= PHPT1, PHP14 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hw4 OCA], [http://www.ebi.ac.uk/pdbsum/2hw4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hw4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Uppenberg, J.]] | [[Category: Uppenberg, J.]] | ||
[[Category: Weigelt, J.]] | [[Category: Weigelt, J.]] | ||
| - | [[Category: FMT]] | ||
[[Category: human]] | [[Category: human]] | ||
[[Category: phosphatase]] | [[Category: phosphatase]] | ||
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[[Category: structural genomics consortium]] | [[Category: structural genomics consortium]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:36:15 2008'' |
Revision as of 00:36, 31 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | PHPT1, PHP14 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human phosphohistidine phosphatase
Overview
Phosphatases are a diverse group of enzymes that regulate numerous cellular processes. Much of what is known relates to the tyrosine, threonine, and serine phosphatases, whereas the histidine phosphatases have not been studied as much. The structure of phosphohistidine phosphatase (PHPT1), the first identified eukaryotic-protein histidine phosphatase, has been determined to a resolution of 1.9A using multiple-wavelength anomalous dispersion methods. This enzyme can dephosphorylate a variety of proteins (e.g. ATP-citrate lyase and the beta-subunit of G proteins). A putative active site has been identified by its electrostatic character, ion binding, and conserved protein residues. Histidine 53 is proposed to play a major role in histidine dephosphorylation based on these observations and previous mutational studies. Models of peptide binding are discussed to suggest possible mechanisms for substrate recognition.
About this Structure
2HW4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
First structure of a eukaryotic phosphohistidine phosphatase., Busam RD, Thorsell AG, Flores A, Hammarstrom M, Persson C, Hallberg BM, J Biol Chem. 2006 Nov 10;281(45):33830-4. Epub 2006 Sep 21. PMID:16990267
Page seeded by OCA on Mon Mar 31 03:36:15 2008
Categories: Homo sapiens | Single protein | Arrowsmith, C. | Berg, S Van Den. | Berglund, H. | Busam, R D. | Collins, R. | Edwards, A. | Ehn, M. | Flodin, S. | Flores, A. | Graslund, S. | Hallberg, B M. | Hammarstrom, M. | Hogbom, M. | Kotenyova, T. | Nilsson-Ehle, P. | Nordlund, P. | Nyman, T. | Ogg, D. | Persson, C. | SGC, Structural Genomics Consortium. | Schiavone, L Holmberg. | Stenmark, P. | Sundstrom, M. | Thorsell, A G. | Uppenberg, J. | Weigelt, J. | Human | Phosphatase | Phosphohistidine | Phpt1 | Sgc | Structural genomic | Structural genomics consortium
