2esb
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2esb |SIZE=350|CAPTION= <scene name='initialview01'>2esb</scene>, resolution 2.Å | |PDB= 2esb |SIZE=350|CAPTION= <scene name='initialview01'>2esb</scene>, resolution 2.Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2esb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2esb OCA], [http://www.ebi.ac.uk/pdbsum/2esb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2esb RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Ryu, S E.]] | [[Category: Ryu, S E.]] | ||
[[Category: Yoon, T S.]] | [[Category: Yoon, T S.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: EPE]] | ||
[[Category: alpha/beta structure]] | [[Category: alpha/beta structure]] | ||
| - | ''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 02:53:08 2008'' |
Revision as of 23:53, 30 March 2008
| |||||||
| , resolution 2.Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human DUSP18
Overview
The human dual-specificity protein phosphatase 18 (DSP18) gene and its protein product have recently been characterized. Like most DSPs, DSP18 displays dephosphorylating activity towards both phosphotyrosine and phosphothreonine residues. However, DSP18 is distinct from other known DSPs in terms of the existence of approximately 30 residues at the C-terminus of the catalytic domain and an unusual optimum activity profile at 328 K. The crystal structure of human DSP18 has been determined at 2.0 A resolution. The catalytic domain of DSP18 adopts a fold similar to that known for other DSP structures. Although good alignments are found with other DSPs, substantial differences are also found in the regions surrounding the active site, suggesting that DSP18 constitutes a unique structure with a distinct substrate specificity. Furthermore, the residues at the C-terminus fold into two antiparallel beta-strands and participate in extensive interactions with the catalytic domain, explaining the thermostability of DSP18.
About this Structure
2ESB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family., Jeong DG, Cho YH, Yoon TS, Kim JH, Son JH, Ryu SE, Kim SJ, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):582-8. Epub 2006, May 12. PMID:16699184
Page seeded by OCA on Mon Mar 31 02:53:08 2008
