5MLO: Human PCNA

Crystal structure of human PCNA in complex with ZRANB3 PIP box peptide. Determined by X-ray diffraction at 1.96 Å resolution. Released 28 Jun 2017.

Method
X-ray diffraction
Resolution
1.96 Å
Organism
Homo sapiens
Chains
6
Atoms
6,705
Mol. weight
92.16 kDa
Released
28 Jun 2017

Explore 5MLO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5MLO contains 33 α-helices and 63 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 8 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand2-651
α-helix10-1910
β-strand25-3172
β-strand34-4072
β-strand46-5382
α-helix54-563
β-strand59-6241
β-strand66-7162
α-helix72-798
β-strand87-9261
β-strand98-10471
β-strand110-11781
β-strand11912
β-strand135-14062
α-helix141-15212
β-strand157-16373
β-strand166-17383
β-strand176-18383
α-helix191-1933
β-strand196-19942
β-strand204-20853
α-helix209-2157
α-helix216-2216
β-strand224-22962
β-strand235-24172
β-strand245-25172
α-helix252-2532
β-strand25413
Chain B: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand51913
α-helix520-5212
α-helix522-5243
Chain C: 10 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand2-654
α-helix10-178
β-strand25-3175
β-strand34-4075
β-strand46-5385
α-helix54-563
β-strand59-6244
β-strand66-7165
α-helix72-798
β-strand87-9264
β-strand98-10474
β-strand110-11784
α-helix1181
β-strand11915
α-helix124-1274
β-strand135-14065
α-helix141-15212
β-strand157-16371
β-strand166-17381
β-strand176-18381
α-helix184-1852
β-strand196-19945
β-strand203-20861
α-helix209-2157
α-helix216-2216
β-strand224-22965
β-strand235-24175
β-strand245-25175
α-helix252-2532
β-strand25411
Chain D: 3 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix5181
β-strand51911
α-helix520-5212
α-helix523-5264
Chain E: 9 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand2-653
α-helix10-1910
β-strand25-3176
β-strand34-4076
β-strand46-5386
α-helix54-563
β-strand59-6243
β-strand66-7166
α-helix72-798
β-strand87-9263
β-strand98-10473
β-strand110-11783
β-strand11916
β-strand135-14066
α-helix141-15212
β-strand157-16264
β-strand166-17384
β-strand176-18384
α-helix184-1852
α-helix191-1933
β-strand196-19946
β-strand203-20864
α-helix209-2157
α-helix216-2216
β-strand224-22966
β-strand235-24176
β-strand245-25176
α-helix252-2532
β-strand25417
Chain F: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand51917
α-helix522-5254

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Proliferating cell nuclear antigenA, C, Eprotein261Homo sapiensP12004 (AlphaFold model)
ZRANB3 PIP box peptideB, D, Fprotein15Homo sapiensQ5FWF4 (AlphaFold model)
Sequence of entity 1 (A, C, E), FASTA
>5MLO_1 Proliferating cell nuclear antigen (chains A, C, E)
MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTY
RCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD
LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNI
KLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYK
IADMGHLKYYLAPKIEDEEGS
Sequence of entity 2 (B, D, F), FASTA
>5MLO_2 ZRANB3 PIP box peptide (chains B, D, F)
EKEKQHDIRSFFVPQ

Primary citation

Structural insights into the function of ZRANB3 in replication stress response. Sebesta, M., Cooper, C.D.O., Ariza, A. et al. Nat Commun (2017) 8:15847-15847. DOI 10.1038/ncomms15847 · PubMed

Other PDB entries of the same protein (UniProt P12004 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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