5MLW: Human PCNA

Crystal structure of human PCNA in complex with ZRANB3 APIM motif peptide. Determined by X-ray diffraction at 2.45 Å resolution. Released 28 Jun 2017.

Method
X-ray diffraction
Resolution
2.45 Å
Organism
Homo sapiens
Chains
6
Atoms
6,348
Mol. weight
90.86 kDa
Released
28 Jun 2017

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

Secondary structure: helices and β-sheets

5MLW contains 27 α-helices and 65 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-helix10-2011
β-strand25-3172
β-strand34-4072
β-strand46-5382
α-helix54-563
β-strand59-6241
β-strand66-7162
α-helix72-809
β-strand87-9261
β-strand98-10471
β-strand110-11781
β-strand11912
β-strand12713
α-helix128-1303
β-strand135-14062
α-helix141-15212
β-strand157-16264
β-strand166-17384
β-strand176-18384
β-strand196-19942
β-strand203-20864
α-helix209-2157
α-helix216-2216
β-strand224-22962
β-strand235-24172
β-strand245-25172
α-helix252-2543
Chains B and D: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix1073-10753
β-strand107713
Chain C: 8 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand2-655
α-helix10-2011
β-strand25-3066
β-strand34-4076
β-strand46-5386
α-helix54-563
β-strand59-6245
β-strand66-7166
α-helix72-809
β-strand87-9265
β-strand98-10475
β-strand110-11785
β-strand11916
β-strand12717
α-helix128-1303
β-strand135-14066
α-helix141-15212
β-strand157-16261
β-strand166-17381
β-strand176-18381
β-strand196-19946
β-strand203-20861
α-helix209-2157
α-helix216-2216
β-strand224-22966
β-strand235-24176
β-strand245-25176
α-helix252-2543
Chain E: 8 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand2-654
α-helix10-2011
β-strand25-3178
β-strand34-4078
β-strand46-5388
α-helix54-563
β-strand59-6244
β-strand66-7168
α-helix72-809
β-strand87-9264
β-strand98-10474
β-strand110-11784
β-strand11918
β-strand12719
α-helix128-1303
β-strand135-14068
α-helix141-15212
β-strand157-16265
β-strand166-17385
β-strand176-18385
β-strand196-19948
β-strand203-20865
α-helix209-2157
α-helix216-2216
β-strand224-22968
β-strand235-24178
β-strand245-25178
α-helix252-2532
β-strand254110
Chain F: 1 helix, 2 β-strands
ElementResiduesLengthSheet
β-strand1070110
α-helix1073-10753
β-strand107719

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Proliferating cell nuclear antigenA, C, Eprotein261Homo sapiensP12004 (AlphaFold model)
APIM motif peptideB, D, Fprotein11Homo sapiensQ5FWF4 (AlphaFold model)
Sequence of entity 1 (A, C, E), FASTA
>5MLW_1 Proliferating cell nuclear antigen (chains A, C, E)
MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTY
RCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD
LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNI
KLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYK
IADMGHLKYYLAPKIEDEEGS
Sequence of entity 2 (B, D, F), FASTA
>5MLW_2 APIM motif peptide (chains B, D, F)
GSDITRFLVKK

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:

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