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1dhp
From Proteopedia
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|PDB= 1dhp |SIZE=350|CAPTION= <scene name='initialview01'>1dhp</scene>, resolution 2.3Å | |PDB= 1dhp |SIZE=350|CAPTION= <scene name='initialview01'>1dhp</scene>, resolution 2.3Å | ||
|SITE= <scene name='pdbsite=S1:Pyruvate+Binding+Residue'>S1</scene> | |SITE= <scene name='pdbsite=S1:Pyruvate+Binding+Residue'>S1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | + | |LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] </span> |
|GENE= DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB]</span> | ||
}} | }} | ||
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[[Category: Korndoerfer, I.]] | [[Category: Korndoerfer, I.]] | ||
[[Category: Mirwaldt, C.]] | [[Category: Mirwaldt, C.]] | ||
| - | [[Category: K]] | ||
[[Category: dihydrodipicolinate]] | [[Category: dihydrodipicolinate]] | ||
[[Category: synthase]] | [[Category: synthase]] | ||
| - | ''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 19:41:45 2008'' |
Revision as of 16:41, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Gene: | DAPA (Escherichia coli) | ||||||
| Activity: | Dihydrodipicolinate synthase, with EC number 4.2.1.52 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIHYDRODIPICOLINATE SYNTHASE
Overview
The crystal structure of dihydrodipicolinate synthase from E. coli was determined by multiple isomorphous replacement methods. The structure was refined at a resolution of 2.5 A and the final R-factor is 19.6% for 32,190 reflections between 10.0 A and 2.5 A and F > 2 sigma (F). The crystallographic asymmetric unit contains two monomers related by approximate 2-fold symmetry. A tetramer with approximate 222 symmetry is built up by crystallographic symmetry. The tetramer is almost planar with no contacts between the subunits related by the non-crystallographic dyad. The active sites are accessible from a wide water-filled channel in the center of the tetramer. The dihydrodipicolinate synthase monomer is composed of two domains. Each polypeptide chain is folded into an 8-fold alpha/beta barrel and a C-terminal alpha-helical domain comprising residues 224 to 292. The fold is similar to that of N-acetylneuraminate lyase. The active site lysine 161 is located in the alpha/beta barrel and has access via two entrances from the C-terminal side of the barrel.
About this Structure
1DHP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution., Mirwaldt C, Korndorfer I, Huber R, J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:7853400
Page seeded by OCA on Sun Mar 30 19:41:45 2008
