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.
1hi9
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1hi9 |SIZE=350|CAPTION= <scene name='initialview01'>1hi9</scene>, resolution 2.40Å | |PDB= 1hi9 |SIZE=350|CAPTION= <scene name='initialview01'>1hi9</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A300'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A301'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+B300'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+B301'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Residue+C300'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Residue+C301'>AC6</scene>, <scene name='pdbsite=AC7:Zn+Binding+Site+For+Residue+D300'>AC7</scene>, <scene name='pdbsite=AC8:Zn+Binding+Site+For+Residue+D301'>AC8</scene>, <scene name='pdbsite=AC9:Zn+Binding+Site+For+Residue+E300'>AC9</scene> and <scene name='pdbsite=BC1:Zn+Binding+Site+For+Residue+E301'>BC1</scene> | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A300'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A301'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+B300'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+B301'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Residue+C300'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Residue+C301'>AC6</scene>, <scene name='pdbsite=AC7:Zn+Binding+Site+For+Residue+D300'>AC7</scene>, <scene name='pdbsite=AC8:Zn+Binding+Site+For+Residue+D301'>AC8</scene>, <scene name='pdbsite=AC9:Zn+Binding+Site+For+Residue+E300'>AC9</scene> and <scene name='pdbsite=BC1:Zn+Binding+Site+For+Residue+E301'>BC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= DCIAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= DCIAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hi9 OCA], [http://www.ebi.ac.uk/pdbsum/1hi9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hi9 RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Goffin, C.]] | [[Category: Goffin, C.]] | ||
[[Category: Remaut, H.]] | [[Category: Remaut, H.]] | ||
| - | [[Category: ZN]] | ||
[[Category: d-aminopeptidase]] | [[Category: d-aminopeptidase]] | ||
[[Category: decamer]] | [[Category: decamer]] | ||
| Line 33: | Line 35: | ||
[[Category: self-compartmentalizing]] | [[Category: self-compartmentalizing]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:05:31 2008'' |
Revision as of 18:05, 30 March 2008
| |||||||
| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | DCIAA (Bacillus subtilis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ZN-DEPENDENT D-AMINOPEPTIDASE DPPA FROM BACILLUS SUBTILIS, A SELF-COMPARTMENTALIZING PROTEASE.
Overview
Bacillus subtilis DppA is a binuclear zinc-dependent, D-specific aminopeptidase. The X-ray structure of the enzyme has been determined at 2.4 A resolution by a three-wavelength MAD experiment. The structure reveals that DppA is a new example of a 'self-compartmentalizing protease', a family of proteolytic complexes. Proteasomes are the most extensively studied representatives of this family. The DppA enzyme is composed of identical 30 kDa subunits organized in a decamer with 52 point-group symmetry. A 20 A wide channel runs through the complex, giving access to a central chamber holding the active sites. The structure shows DppA to be a prototype of a new family of metalloaminopeptidases characterized by the SXDXEG key sequence.
About this Structure
1HI9 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease., Remaut H, Bompard-Gilles C, Goffin C, Frere JM, Van Beeumen J, Nat Struct Biol. 2001 Aug;8(8):674-8. PMID:11473256
Page seeded by OCA on Sun Mar 30 21:05:31 2008
