Crystal structure of Human MCM2 HBD and ASF1b chaperoning a histone H3.2-H4 dimer

Summary for 5BO0

Related5BNV 5BNX
DescriptorHistone H3.2, Histone H4, DNA replication licensing factor MCM2, ... (5 entities in total)
Functional Keywordsdna replication, mcm2, asf1b, h3.2-h4 dimer, chaperone-dna binding protein complex, chaperone/dna binding protein
Biological sourceHomo sapiens (Human)
Cellular locationNucleus Q71DI3 P62805 P49736 Q9NVP2
Total number of polymer chains4
Total molecular weight46362.58
Huang, H.,Patel, D.J. (deposition date: 2015-05-26, release date: 2015-06-17, Last modification date: 2015-08-19)
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 (PDB entries with the same primary citation)
DOI: 10.1038/nsmb.3055
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.23880 6.4% 2.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-09-23