The Crystal Structure of Human Porphobilinogen Deaminase at 2.8A resolution

Summary for 3EQ1

DescriptorPorphobilinogen deaminase, 3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1H-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1H-pyrrol-3-yl]propanoic acid, SULFATE ION (3 entities in total)
Functional Keywordsalpha and beta protein, alternative splicing, cytoplasm, disease mutation, heme biosynthesis, porphyrin biosynthesis, transferase
Biological sourceHomo sapiens (Human)
Cellular locationCytoplasm (Probable) P08397
Total number of polymer chains2
Total molecular weight80221.16
Kolstoe, S.E.,Gill, R.,Mohammed, F.,Wood, S.P. (deposition date: 2008-09-30, release date: 2009-03-03, Last modification date: 2011-07-13)
Primary citation
Gill, R.,Kolstoe, S.E.,Mohammed, F.,Al D-Bass, A.,Mosely, J.E.,Sarwar, M.,Cooper, J.B.,Wood, S.P.,Shoolingin-Jordan, P.M.
Structure of human porphobilinogen deaminase at 2.8 A: the molecular basis of acute intermittent porphyria
Biochem.J., 420:17-25, 2009
PubMed: 19207107 (PDB entries with the same primary citation)
DOI: 10.1042/BJ20082077
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.2871005.0%2.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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