5BNV

Crystal structure of Human MCM2 HBD chaperoning a histone H3-H4 tetramer

Summary for 5BNV

• Entry DOI: 10.2210/pdb5bnv/pdb
• Related: 5BNX 5BO0
• Descriptor: Histone H3.3, Histone H4, DNA replication licensing factor MCM2, ... (5 entities in total)
• Functional Keywords: dna replication, mcm2 helicase, histone chaperone, h3-h4 tetramer, chaperone-dna binding protein complex, chaperone/dna binding protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus: P84243 P62805 P49736
• Total number of polymer chains: 6
• Total formula weight: 56585.07

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; PubMed: 26167883; DOI: 10.1038/nsmb.3055

Experimental method

X-RAY DIFFRACTION (2.795 Å)