4DL1
Crystal Structure of human Myeloperoxidase with covalent thioxanthine analog
Summary for 4DL1
Entry DOI | 10.2210/pdb4dl1/pdb |
Descriptor | Myeloperoxidase light chain, Myeloperoxidase heavy chain, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
Functional Keywords | oxidoreductase, heme-dependent peroxidase |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 16 |
Total formula weight | 541355.54 |
Authors | Vajdos, F.,Varghese, A. (deposition date: 2012-02-05, release date: 2012-03-21, Last modification date: 2020-07-29) |
Primary citation | Geoghegan, K.F.,Varghese, A.H.,Feng, X.,Bessire, A.J.,Conboy, J.J.,Ruggeri, R.B.,Ahn, K.,Spath, S.N.,Filippov, S.V.,Conrad, S.J.,Carpino, P.A.,Guimaraes, C.R.,Vajdos, F.F. Deconstruction of activity-dependent covalent modification of heme in human neutrophil myeloperoxidase by multistage mass spectrometry (MS(4)). Biochemistry, 51:2065-2077, 2012 Cited by PubMed: 22352991DOI: 10.1021/bi201872j PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report