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1XNA
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BU of 1xna by Molmil
NMR SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK REPAIR PROTEIN XRCC1-N-TERMINAL DOMAIN
Descriptor: PROTEIN (DNA-REPAIR PROTEIN XRCC1)
Authors:Marintchev, A, Mullen, G.P.
Deposit date:1999-02-27
Release date:1999-09-01
Last modified:2023-12-27
Method:SOLUTION NMR
Cite:Solution structure of the single-strand break repair protein XRCC1 N-terminal domain.
Nat.Struct.Biol., 6, 1999
1XNT
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BU of 1xnt by Molmil
NMR SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK REPAIR PROTEIN XRCC1-N-TERMINAL DOMAIN
Descriptor: PROTEIN (DNA-REPAIR PROTEIN XRCC1)
Authors:Marintchev, A, Mullen, G.P.
Deposit date:1999-02-27
Release date:1999-09-01
Last modified:2023-12-27
Method:SOLUTION NMR
Cite:Solution structure of the single-strand break repair protein XRCC1 N-terminal domain.
Nat.Struct.Biol., 6, 1999
3K75
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BU of 3k75 by Molmil
X-ray crystal structure of reduced XRCC1 bound to DNA pol beta catalytic domain
Descriptor: DNA polymerase beta, DNA repair protein XRCC1
Authors:Cuneo, M.J, London, R.E.
Deposit date:2009-10-12
Release date:2010-04-28
Last modified:2024-02-21
Method:X-RAY DIFFRACTION (2.95 Å)
Cite:Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity.
Proc.Natl.Acad.Sci.USA, 107, 2010
3K77
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BU of 3k77 by Molmil
X-ray crystal structure of XRCC1
Descriptor: DNA repair protein XRCC1
Authors:Cuneo, M.J, London, R.E.
Deposit date:2009-10-12
Release date:2010-04-28
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (2.597 Å)
Cite:Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity.
Proc.Natl.Acad.Sci.USA, 107, 2010
3LQC
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BU of 3lqc by Molmil
X-ray crystal structure of oxidized XRCC1 bound to DNA pol beta Palm thumb domain
Descriptor: CARBONATE ION, DNA polymerase beta, DNA repair protein XRCC1, ...
Authors:Cuneo, M.J, Krahn, J.M, London, R.E.
Deposit date:2010-02-09
Release date:2010-04-28
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (2.349 Å)
Cite:Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity.
Proc.Natl.Acad.Sci.USA, 107, 2010

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