General information
PDB ID 6EHT
Title MODULATION OF PCNA SLIDING SURFACE BY P15PAF SUGGESTS A SUPPRESSIVE MECHANISM FOR CISPLATIN-INDUCED DNA LESION BYPASS BY POL ETA HOLOENZYME
PDB header DNA BINDING PROTEIN
Date 2017-09-15
Experimental method X-RAY DIFFRACTION
Resolution (A) 3.2
Kind dna
Organism HOMO SAPIENS
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PDB PDBe MMDB Jena OCA
CATH PDBsum HSSP PDBePISA UniProt
ProteopediA BIPA
Composition of PDB entry and biounits
File: Protein chains: DNA chains: RNA chains: No. of models: Action:
PDB entry:
pdb6eht.pdb ABCDE FG 0
Biounits:
6eht.pdb1.pdb ABCDE FG 1
Pfam domains
Name: Type: Domain: E-value: Significance: Clan: Prot. chain: Start res.: End res.: Nuc. chains: Int. mode: Action:
PCNA_C Domain P12004_127-254 5.2e-63 1 CL0060 A 127 254   
PCNA_N Domain P12004_1-125 3.9e-60 1 CL0060 A 1 125 F  L-Bb 
PCNA_C Domain P12004_127-254 5.2e-63 1 CL0060 B 127 254   
PCNA_N Domain P12004_1-125 3.7e-59 1 CL0060 B 2 125   
PCNA_C Domain P12004_127-254 5.3e-63 1 CL0060 C 127 254   
PCNA_N Domain P12004_1-125 3.9e-60 1 CL0060 C 1 125   
PAF Domain Q15004_52-71 1.2e-09 1 CL0012 D 52 71   
PAF Domain Q15004_52-71 5.2e-09 1 CL0012 E 53 71   
SCOP domains
No SCOP domains
GO terms
Protein chains: GO type: GO description:
A/B=1-254, C=1-255 C centrosome
A/B=1-254, C=1-255 C chromatin
A/B=1-254, C=1-255 C cyclin-dependent protein kinase holoenzyme complex
A/B=1-254, C=1-255 C extracellular exosome
A/B=1-254, C=1-255 C nuclear body
A/B=1-254, C=1-255 C nuclear chromosome, telomeric region
A/B=1-254, C=1-255 C nuclear lamina
A/B=1-254, C=1-255 C nuclear replication fork
A/B=1-254, C=1-255 C nucleoplasm
A/B=1-254, C=1-255 C nucleus
A/B=1-254, C=1-255 C PCNA complex
A/B=1-254, C=1-255 C PCNA-p21 complex
A/B=1-254, C=1-255 C replication fork
A/B=1-254, C=1-255 C replisome
A/B=1-254, C=1-255 F chromatin binding
A/B=1-254, C=1-255 F damaged DNA binding
A/B=1-254, C=1-255 F dinucleotide insertion or deletion binding
A/B=1-254, C=1-255 F DNA polymerase binding
A/B=1-254, C=1-255 F DNA polymerase processivity factor activity
A/B=1-254, C=1-255 F enzyme binding
A/B=1-254, C=1-255 F estrogen receptor binding
A/B=1-254, C=1-255 F histone acetyltransferase binding
A/B=1-254, C=1-255 F identical protein binding
A/B=1-254, C=1-255 F MutLalpha complex binding
A/B=1-254, C=1-255 F protein C-terminus binding
A/B=1-254, C=1-255 F protein-containing complex binding
A/B=1-254, C=1-255 F purine-specific mismatch base pair DNA N-glycosylase activity
A/B=1-254, C=1-255 F receptor tyrosine kinase binding
A/B=1-254, C=1-255 P base-excision repair, gap-filling
A/B=1-254, C=1-255 P cellular response to hydrogen peroxide
A/B=1-254, C=1-255 P cellular response to UV
A/B=1-254, C=1-255 P cellular response to xenobiotic stimulus
A/B=1-254, C=1-255 P DNA damage response, detection of DNA damage
A/B=1-254, C=1-255 P DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
A/B=1-254, C=1-255 P epithelial cell differentiation
A/B=1-254, C=1-255 P error-free translesion synthesis
A/B=1-254, C=1-255 P error-prone translesion synthesis
A/B=1-254, C=1-255 P estrous cycle
A/B=1-254, C=1-255 P heart development
A/B=1-254, C=1-255 P leading strand elongation
A/B=1-254, C=1-255 P liver regeneration
A/B=1-254, C=1-255 P mismatch repair
A/B=1-254, C=1-255 P mitotic telomere maintenance via semi-conservative replication
A/B=1-254, C=1-255 P negative regulation of transcription by RNA polymerase II
A/B=1-254, C=1-255 P nucleotide-excision repair, DNA gap filling
A/B=1-254, C=1-255 P nucleotide-excision repair, DNA incision
A/B=1-254, C=1-255 P nucleotide-excision repair, DNA incision, 5'-to lesion
A/B=1-254, C=1-255 P positive regulation of deoxyribonuclease activity
A/B=1-254, C=1-255 P positive regulation of DNA repair
A/B=1-254, C=1-255 P positive regulation of DNA replication
A/B=1-254, C=1-255 P positive regulation of DNA-directed DNA polymerase activity
A/B=1-254, C=1-255 P protein ubiquitination
A/B=1-254, C=1-255 P regulation of transcription involved in G1/S transition of mitotic cell cycle
A/B=1-254, C=1-255 P replication fork processing
A/B=1-254, C=1-255 P response to cadmium ion
A/B=1-254, C=1-255 P response to dexamethasone
A/B=1-254, C=1-255 P response to estradiol
A/B=1-254, C=1-255 P response to L-glutamate
A/B=1-254, C=1-255 P telomere maintenance
A/B=1-254, C=1-255 P telomere maintenance via semi-conservative replication
A/B=1-254, C=1-255 P transcription-coupled nucleotide-excision repair
A/B=1-254, C=1-255 P translesion synthesis
A/B=1-254, C=1-255 P viral process
D/E=52-71 C centrosome
D/E=52-71 C nucleoplasm
D/E=52-71 C nucleus
D/E=52-71 C perinuclear region of cytoplasm
D/E=52-71 F chromatin binding
D/E=52-71 P cellular response to DNA damage stimulus
D/E=52-71 P centrosome cycle
D/E=52-71 P DNA replication
D/E=52-71 P regulation of cell cycle
D/E=52-71 P response to UV
D/E=52-71 P translesion synthesis
Sequences
Download file with secondary structure created by Stride  
6eht.pdb1.pdb:   [ download sequences in FASTA format ]
F (dna): 
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G (dna): 
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A (protein): 
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B (protein): 
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C (protein): 
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D (protein): 
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E (protein): 
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