1pda: Difference between revisions
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|PDB= 1pda |SIZE=350|CAPTION= <scene name='initialview01'>1pda</scene>, resolution 1.76Å | |PDB= 1pda |SIZE=350|CAPTION= <scene name='initialview01'>1pda</scene>, resolution 1.76Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=DPM:3-{2-[4-(2-CARBOXY-ETHYL)-3-CARBOXYMETHYL-5H-PYRROL-2-YLMETHYL]-4-CARBOXYMETHYL-5-METHYL-2H-PYRROL-3-YL}-PROPIONIC+ACID'>DPM</scene> | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=DPM:3-{2-[4-(2-CARBOXY-ETHYL)-3-CARBOXYMETHYL-5H-PYRROL-2-YLMETHYL]-4-CARBOXYMETHYL-5-METHYL-2H-PYRROL-3-YL}-PROPIONIC+ACID'>DPM</scene> | ||
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxymethylbilane_synthase Hydroxymethylbilane synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.61 2.5.1.61] </span> | |||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pda OCA], [http://www.ebi.ac.uk/pdbsum/1pda PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pda RCSB]</span> | |||
}} | }} | ||
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[[Category: Wood, S P.]] | [[Category: Wood, S P.]] | ||
[[Category: Woodcock, S C.]] | [[Category: Woodcock, S C.]] | ||
[[Category: lyase(porphyrin)]] | [[Category: lyase(porphyrin)]] | ||
''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 22:58:07 2008'' | ||
Revision as of 19:58, 30 March 2008
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| 1pda, resolution 1.76Å | |||||||||||||
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| Ligands: | ACY, DPM | ||||||||||||
| Activity: | Hydroxymethylbilane synthase, with EC number 2.5.1.61 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF PORPHOBILINOGEN DEAMINASE REVEALS A FLEXIBLE MULTIDOMAIN POLYMERASE WITH A SINGLE CATALYTIC SITE
Overview
The three-domain structure of porphobilinogen deaminase, a key enzyme in the biosynthetic pathway of tetrapyrroles, has been defined by X-ray analysis at 1.9 A resolution. Two of the domains structurally resemble the transferrins and periplasmic binding proteins. The dipyrromethane cofactor is covalently linked to domain 3 but is bound by extensive salt-bridges and hydrogen-bonds within the cleft between domains 1 and 2, at a position corresponding to the binding sites for small-molecule ligands in the analogous proteins. The X-ray structure and results from site-directed mutagenesis provide evidence for a single catalytic site. Interdomain flexibility may aid elongation of the polypyrrole product in the active-site cleft of the enzyme.
About this Structure
1PDA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site., Louie GV, Brownlie PD, Lambert R, Cooper JB, Blundell TL, Wood SP, Warren MJ, Woodcock SC, Jordan PM, Nature. 1992 Sep 3;359(6390):33-9. PMID:1522882
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