4EXT
Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta
Summary for 4EXT
Entry DOI | 10.2210/pdb4ext/pdb |
Descriptor | DNA repair protein REV1, peptide from DNA polymerase zeta catalytic subunit, Mitotic spindle assembly checkpoint protein MAD2B, ... (4 entities in total) |
Functional Keywords | rev1, rev3, rev7, polymerase-interacting domain, y-family polymerase, b-family polymerase, translesional synthesis polymerase, dna damage tolerance, scaffold, transferase-transcription complex, transferase/transcription |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus (Probable): Q9UBZ9 Nucleus (Potential): O60673 Nucleus: Q9UI95 |
Total number of polymer chains | 3 |
Total formula weight | 37327.50 |
Authors | Liu, D.N.,Ryu, K.S.,Ko, J.S.,Choi, B.S. (deposition date: 2012-05-01, release date: 2013-05-08, Last modification date: 2024-03-20) |
Primary citation | Liu, D.N.,Ryu, K.S.,Ko, J.S.,Choi, B.S. Insights into the scaffold mechanism of human Rev1 in translesional synthesis revealed by structural studies on its polymerase-interacting domain To be Published, |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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