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DP00003 - DNA-binding protein

Organism Human adenovirus C serotype 5
Gene DBP
Sequence length 529
Disorder content 9.8%
Cross references UniProtKB:P03265, MobiDB:P03265
Dataset(s) Viral proteins
Last update 2022-02-14
Entry history
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50100150200250300350400450500DisProt consensusStructural state
Example filters structural state transition interaction partner disorder function magnetic resonance
Selected regions 2 / 2
DP00003r004 Structural state
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Term disorder, IDPO:00076
Fragment 454 - 464
Evidence X-ray crystallography-based structural model with missing residue coordinates used in manual assertion, ECO:0006220
Cross references PDB:1ADV PDB:1ADU
Reference Alternative arrangements of the protein chain are possible for the adenovirus single-stranded DNA binding protein. Kanellopoulos PN, Tsernoglou D, van der Vliet PC, Tucker PA. J Mol Biol, 1996, pmid:8632448
Statements Article "Five sections of the polypeptidechain are either invisible, or poorly defined in the electron density map. For the first molecule of the dimer in the asymmetric unit they are A174 to A179 (the N terminus of the C-terminal domain), A294 to A334, A401 to A405, A427 to A432 and A454 to A464 whilst for the second molecule they are B174 to B179, B293 to B334, B344 to B349, B401 to B405 and B454 to B464."
Curator Federica Quaglia
validated by Edoardo Salladini
DP00003r002 Structural state
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Term disorder, IDPO:00076
Fragment 294 - 334
Evidence X-ray crystallography-based structural model with missing residue coordinates used in manual assertion, ECO:0006220
Cross references PDB:1ADV PDB:1ADU
Reference Alternative arrangements of the protein chain are possible for the adenovirus single-stranded DNA binding protein. Kanellopoulos PN, Tsernoglou D, van der Vliet PC, Tucker PA. J Mol Biol, 1996, pmid:8632448
Statements Article "Five sections of the polypeptidechain are either invisible, or poorly defined in the electron density map. For the first molecule of the dimer in the asymmetric unit they are A174 to A179 (the N terminus of the C-terminal domain), A294 to A334, A401 to A405, A427 to A432 and A454 to A464 whilst for the second molecule they are B174 to B179, B293 to B334, B344 to B349, B401 to B405 and B454 to B464."
Curator Federica Quaglia
validated by Edoardo Salladini
BioComputing UP, 2021 - University of Padua, Italy
License and disclaimer
This database is part of a project that has received funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 778247.
University of Padua
Department of Biomedical Sciences
ELIXIR Europe
IDPfun
Non-globular proteins - COST Action BM1405