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
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-6 | 5 | 1 |
| α-helix | 10-19 | 10 | |
| β-strand | 25-31 | 7 | 2 |
| β-strand | 34-40 | 7 | 2 |
| β-strand | 46-53 | 8 | 2 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 1 |
| β-strand | 66-71 | 6 | 2 |
| α-helix | 72-79 | 8 | |
| β-strand | 87-92 | 6 | 1 |
| β-strand | 98-104 | 7 | 1 |
| β-strand | 110-117 | 8 | 1 |
| β-strand | 119 | 1 | 2 |
| β-strand | 135-140 | 6 | 2 |
| α-helix | 141-152 | 12 | |
| β-strand | 157-163 | 7 | 3 |
| β-strand | 166-173 | 8 | 3 |
| β-strand | 176-183 | 8 | 3 |
| α-helix | 191-193 | 3 | |
| β-strand | 196-199 | 4 | 2 |
| β-strand | 204-208 | 5 | 3 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-229 | 6 | 2 |
| β-strand | 235-241 | 7 | 2 |
| β-strand | 245-251 | 7 | 2 |
| α-helix | 252-253 | 2 | |
| β-strand | 254 | 1 | 3 |
Chain B: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 519 | 1 | 3 |
| α-helix | 520-521 | 2 | |
| α-helix | 522-524 | 3 | |
Chain C: 10 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-6 | 5 | 4 |
| α-helix | 10-17 | 8 | |
| β-strand | 25-31 | 7 | 5 |
| β-strand | 34-40 | 7 | 5 |
| β-strand | 46-53 | 8 | 5 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 4 |
| β-strand | 66-71 | 6 | 5 |
| α-helix | 72-79 | 8 | |
| β-strand | 87-92 | 6 | 4 |
| β-strand | 98-104 | 7 | 4 |
| β-strand | 110-117 | 8 | 4 |
| α-helix | 118 | 1 | |
| β-strand | 119 | 1 | 5 |
| α-helix | 124-127 | 4 | |
| β-strand | 135-140 | 6 | 5 |
| α-helix | 141-152 | 12 | |
| β-strand | 157-163 | 7 | 1 |
| β-strand | 166-173 | 8 | 1 |
| β-strand | 176-183 | 8 | 1 |
| α-helix | 184-185 | 2 | |
| β-strand | 196-199 | 4 | 5 |
| β-strand | 203-208 | 6 | 1 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-229 | 6 | 5 |
| β-strand | 235-241 | 7 | 5 |
| β-strand | 245-251 | 7 | 5 |
| α-helix | 252-253 | 2 | |
| β-strand | 254 | 1 | 1 |
Chain D: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 518 | 1 | |
| β-strand | 519 | 1 | 1 |
| α-helix | 520-521 | 2 | |
| α-helix | 523-526 | 4 | |
Chain E: 9 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-6 | 5 | 3 |
| α-helix | 10-19 | 10 | |
| β-strand | 25-31 | 7 | 6 |
| β-strand | 34-40 | 7 | 6 |
| β-strand | 46-53 | 8 | 6 |
| α-helix | 54-56 | 3 | |
| β-strand | 59-62 | 4 | 3 |
| β-strand | 66-71 | 6 | 6 |
| α-helix | 72-79 | 8 | |
| β-strand | 87-92 | 6 | 3 |
| β-strand | 98-104 | 7 | 3 |
| β-strand | 110-117 | 8 | 3 |
| β-strand | 119 | 1 | 6 |
| β-strand | 135-140 | 6 | 6 |
| α-helix | 141-152 | 12 | |
| β-strand | 157-162 | 6 | 4 |
| β-strand | 166-173 | 8 | 4 |
| β-strand | 176-183 | 8 | 4 |
| α-helix | 184-185 | 2 | |
| α-helix | 191-193 | 3 | |
| β-strand | 196-199 | 4 | 6 |
| β-strand | 203-208 | 6 | 4 |
| α-helix | 209-215 | 7 | |
| α-helix | 216-221 | 6 | |
| β-strand | 224-229 | 6 | 6 |
| β-strand | 235-241 | 7 | 6 |
| β-strand | 245-251 | 7 | 6 |
| α-helix | 252-253 | 2 | |
| β-strand | 254 | 1 | 7 |
Chain F: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 519 | 1 | 7 |
| α-helix | 522-525 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Proliferating cell nuclear antigen | A, C, E | protein | 261 | Homo sapiens | P12004 (AlphaFold model) |
| ZRANB3 PIP box peptide | B, D, F | protein | 15 | Homo sapiens | Q5FWF4 (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:
- 1U7B 1.88 Å, Crystal structure of hPCNA bound to residues 331-350 of the flap endonuclease-1 (FEN1)
- 8F5Q 1.9 Å, Crystal structure of human PCNA in complex with the PIP box of FBH1
- 9N3L 1.9 Å, Co-crystal structure of PCNA bound to HSP90alpha inhibitor, SNX2112
- 5E0U 1.93 Å, Human PCNA variant (S228I) complexed with p21 at 1.9 Angstroms
- 4RJF 2.01 Å, Crystal structure of the human sliding clamp at 2.0 angstrom resolution
- 5E0V 2.07 Å, Human PCNA variant (S228I) complexed with FEN1 at 2.1 Angstroms
- 3VKX 2.1 Å, Structure of PCNA
- 6HVO 2.1 Å, Crystal structure of human PCNA in complex with three peptides of p12 subunit of human…
- 4ZTD 2.2 Å, Crystal Structure of Human PCNA in complex with a TRAIP peptide
- 5YCO 2.2 Å, Complex structure of PCNA with UHRF2
- 5MOM 2.27 Å, Crystal Structure of PCNA encoding the hypomorphic mutation S228I
- 1VYM 2.3 Å, Native human pcna
Browse structure collections
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