4ZTD: Human PCNA

Crystal Structure of Human PCNA in complex with a TRAIP peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 Dec 2015.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
6
Atoms
6,245
Mol. weight
86.92 kDa
Released
16 Dec 2015

Explore 4ZTD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ZTD contains 26 α-helices and 57 β-strands across 5 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: 9 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand4-631
α-helix9-179
β-strand25-3172
β-strand34-4072
β-strand46-5382
α-helix54-563
β-strand59-6021
β-strand66-7162
α-helix72-798
α-helix861
β-strand87-9151
β-strand98-10471
β-strand110-11781
β-strand11912
α-helix128-1303
β-strand135-14062
α-helix141-15212
β-strand157-16263
β-strand166-17383
β-strand176-18383
α-helix184-1852
β-strand196-19942
β-strand203-20863
α-helix209-2157
α-helix216-2216
β-strand224-22962
β-strand235-24172
β-strand245-25172
Chain B: 8 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-644
α-helix9-179
β-strand25-3175
β-strand34-4075
β-strand46-5385
α-helix54-563
β-strand59-6134
β-strand66-7165
α-helix72-809
β-strand87-9264
β-strand98-10474
β-strand110-11784
α-helix1181
β-strand11915
β-strand135-14065
α-helix141-15212
β-strand157-16261
β-strand166-17271
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
Chain C: 6 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-643
α-helix9-2012
β-strand25-3176
β-strand34-4076
β-strand46-5386
α-helix54-563
β-strand59-6133
β-strand66-7166
α-helix72-809
β-strand87-9153
β-strand98-10473
β-strand110-11783
β-strand11916
β-strand135-14066
α-helix141-15414
β-strand157-16264
β-strand166-17274
β-strand176-18384
β-strand196-19946
β-strand203-20864
α-helix209-2157
α-helix216-2216
β-strand224-22966
β-strand235-24176
β-strand245-25176
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix463-4653
Chain E: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix460-4623
α-helix464-4663

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Proliferating cell nuclear antigenA, B, Cprotein253Homo sapiensP12004 (AlphaFold model)
Ala-phe-gln-ala-lys-leu-asp-thr-phe-leu-trp-serD, Eprotein12Homo sapiensQ9BWF2 (AlphaFold model)
Ala-gly-ala-gly-alaFprotein5Homo sapiens
Sequence of entity 1 (A, B, C), FASTA
>4ZTD_1 Proliferating cell nuclear antigen (chains A, B, C)
FEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYR
CDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDL
DVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIK
LSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKI
ADMGHLKYYLAPK
Sequence of entity 2 (D, E), FASTA
>4ZTD_2 ALA-PHE-GLN-ALA-LYS-LEU-ASP-THR-PHE-LEU-TRP-SER (chains D, E)
AFQAKLDTFLWS
Sequence of entity 3 (F), FASTA
>4ZTD_3 ALA-GLY-ALA-GLY-ALA (chains F)
AGAGA

Primary citation

TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress. Hoffmann, S., Smedegaard, S., Nakamura, K. et al. J Cell Biol (2016) 212:63-75. DOI 10.1083/jcb.201506071 · 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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