1zpd

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File:1zpd.png

1zpd, resolution 1.86Å ()

Ligands:

, ,

Activity:

Pyruvate decarboxylase, with EC number 4.1.1.1

Structural annotation:
Resources:	CATH : 1Zpda01, 1Zpda03, 1Zpda02, 1Zpdb01, 1Zpdb02, 1Zpdb03, 1Zpde02, 1Zpde03, 1Zpde01, 1Zpdf03, 1Zpdf01, 1Zpdf02 InterPro : Ipr012000, Ipr000399, Ipr012001, Ipr011766, Ipr012110 Pfam : PF02775, PF02776, PF00205 SCOP : d1zpda1, d1zpda3, d1zpda2, d1zpdb1, d1zpdb3, d1zpdb2, d1zpde3, d1zpde2, d1zpde1, d1zpdf1, d1zpdf2, d1zpdf3 UniProt : P06672

Functional annotation:
Molecular function:	magnesium ion binding carboxy-lyase activity thiamin pyrophosphate binding lyase activity pyruvate decarboxylase activity metal ion binding transferase activity catalytic activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILISPYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS

Template:ABSTRACT PUBMED 9685367

About this StructureAbout this Structure

1ZPD is a 4 chains structure of sequences from Zymomonas mobilis. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}

↑ Dobritzsch D, Konig S, Schneider G, Lu G. High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases. J Biol Chem. 1998 Aug 7;273(32):20196-204. PMID:9685367

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OCA

[1] Dobritzsch D, Konig S, Schneider G, Lu G. High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases. J Biol Chem. 1998 Aug 7;273(32):20196-204. PMID:9685367

[xtra 1]