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1PT1

Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with Histidine 11 Mutated to Alanine

Summary for 1PT1
Entry DOI10.2210/pdb1pt1/pdb
Related1PPY 1PQE 1PQF 1PQH 1PT0 1PYQ 1PYU 1aw8
DescriptorAspartate 1-decarboxylase, SULFATE ION (3 entities in total)
Functional Keywordsdecarboxylase, pantothenate pathway, protein self-processing, lyase
Biological sourceEscherichia coli
Cellular locationCytoplasm: P0A790
Total number of polymer chains2
Total formula weight31809.92
Authors
Schmitzberger, F.,Kilkenny, M.L.,Lobley, C.M.C.,Webb, M.E.,Vinkovic, M.,Matak-Vinkovic, D.,Witty, M.,Chirgadze, D.Y.,Smith, A.G.,Abell, C.,Blundell, T.L. (deposition date: 2003-06-22, release date: 2003-11-11, Last modification date: 2023-08-16)
Primary citationSchmitzberger, F.,Kilkenny, M.L.,Lobley, C.M.C.,Webb, M.E.,Vinkovic, M.,Matak-Vinkovic, D.,Witty, M.,Chirgadze, D.Y.,Smith, A.G.,Abell, C.,Blundell, T.L.
Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase
Embo J., 22:6193-6204, 2003
Cited by
PubMed: 14633979
DOI: 10.1093/emboj/cdg575
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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