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1pda

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|PDB= 1pda |SIZE=350|CAPTION= <scene name='initialview01'>1pda</scene>, resolution 1.76&Aring;
|PDB= 1pda |SIZE=350|CAPTION= <scene name='initialview01'>1pda</scene>, resolution 1.76&Aring;
|SITE=
|SITE=
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|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> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|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>
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|ACTIVITY= [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]
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|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=
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|DOMAIN=
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|RELATEDENTRY=
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|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.]]
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[[Category: ACY]]
 
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[[Category: DPM]]
 
[[Category: lyase(porphyrin)]]
[[Category: lyase(porphyrin)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:56 2008''
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''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

Image:1pda.jpg


PDB ID 1pda

Drag the structure with the mouse to rotate
, resolution 1.76Å
Ligands: ,
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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