5BO0
Crystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.2-H4 dimer
Summary for 5BO0
Entry DOI | 10.2210/pdb5bo0/pdb |
Related | 5BNV 5BNX |
Descriptor | Histone H3.2, Histone H4, DNA replication licensing factor MCM2, ... (5 entities in total) |
Functional Keywords | dna replication, mcm2, asf1b, h3.2-h4 dimer, chaperone-dna binding protein complex, chaperone/dna binding protein |
Biological source | Homo sapiens (Human) More |
Cellular location | Nucleus: Q71DI3 P62805 P49736 Q9NVP2 |
Total number of polymer chains | 4 |
Total formula weight | 46362.58 |
Authors | Huang, H.,Patel, D.J. (deposition date: 2015-05-26, release date: 2015-06-17, Last modification date: 2024-03-06) |
Primary citation | Huang, H.,Strmme, C.B.,Saredi, G.,Hodl, M.,Strandsby, A.,Gonzalez-Aguilera, C.,Chen, S.,Groth, A.,Patel, D.J. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nat.Struct.Mol.Biol., 22:618-626, 2015 Cited by PubMed: 26167883DOI: 10.1038/nsmb.3055 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.906 Å) |
Structure validation
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