3II6: Human Xrcc4
Structure of human Xrcc4 in complex with the tandem BRCT domains of DNA LigaseIV. Determined by X-ray diffraction at 2.4 Å resolution. Released 11 Aug 2009.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 10,925
- Mol. weight
- 154.21 kDa
- Released
- 11 Aug 2009
Explore 3II6 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3II6 contains 40 α-helices and 65 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: 3 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-10 | 8 | 1 |
| β-strand | 13-23 | 11 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 42-44 | 3 | 1 |
| β-strand | 46-48 | 3 | 1 |
| α-helix | 49-58 | 10 | |
| α-helix | 63-74 | 12 | |
| β-strand | 84-88 | 5 | 2 |
| β-strand | 94-100 | 7 | 2 |
| β-strand | 105-112 | 8 | 2 |
| β-strand | 114-115 | 2 | 1 |
| α-helix | 119-200 | 82 | |
Chain B: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-8 | 7 | 3 |
| β-strand | 18-25 | 8 | 3 |
| β-strand | 27-37 | 11 | 3 |
| β-strand | 42-43 | 2 | 3 |
| β-strand | 46 | 1 | 3 |
| α-helix | 55-58 | 4 | |
| α-helix | 64-74 | 11 | |
| β-strand | 86-88 | 3 | 4 |
| β-strand | 94-97 | 4 | 4 |
| β-strand | 109-112 | 4 | 4 |
| α-helix | 119-200 | 82 | |
Chain C: 3 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-10 | 8 | 5 |
| β-strand | 13-23 | 11 | 5 |
| β-strand | 25 | 1 | 6 |
| β-strand | 27 | 1 | 6 |
| β-strand | 31-37 | 7 | 5 |
| β-strand | 42-44 | 3 | 5 |
| β-strand | 46-48 | 3 | 5 |
| α-helix | 49-58 | 10 | |
| α-helix | 65-74 | 10 | |
| β-strand | 84-89 | 6 | 7 |
| β-strand | 94-101 | 8 | 7 |
| β-strand | 104-112 | 9 | 7 |
| β-strand | 114-115 | 2 | 5 |
| α-helix | 119-199 | 81 | |
Chain D: 3 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-8 | 7 | 8 |
| β-strand | 18-25 | 8 | 8 |
| β-strand | 27-37 | 11 | 8 |
| β-strand | 42-46 | 5 | 8 |
| α-helix | 55-58 | 4 | |
| α-helix | 63-74 | 12 | |
| β-strand | 86-88 | 3 | 9 |
| β-strand | 94-97 | 4 | 9 |
| β-strand | 109-112 | 4 | 9 |
| α-helix | 121-199 | 79 | |
Chain X: 13 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 663-666 | 4 | 10 |
| α-helix | 675-684 | 10 | |
| β-strand | 688-689 | 2 | 10 |
| β-strand | 697-701 | 5 | 10 |
| α-helix | 707-714 | 8 | |
| β-strand | 720-721 | 2 | 10 |
| α-helix | 723-732 | 10 | |
| α-helix | 740-742 | 3 | |
| β-strand | 743-745 | 3 | 10 |
| α-helix | 748-753 | 6 | |
| β-strand | 758 | 1 | 11 |
| β-strand | 764 | 1 | 11 |
| α-helix | 771-779 | 9 | |
| α-helix | 789-803 | 15 | |
| α-helix | 809-811 | 3 | |
| β-strand | 817-820 | 4 | 12 |
| β-strand | 823 | 1 | 13 |
| α-helix | 829-831 | 3 | |
| β-strand | 832 | 1 | 13 |
| α-helix | 837-847 | 11 | |
| β-strand | 851-853 | 3 | 12 |
| β-strand | 858 | 1 | 14 |
| β-strand | 860 | 1 | 14 |
| β-strand | 862-865 | 4 | 12 |
| α-helix | 872-880 | 9 | |
| β-strand | 887-890 | 4 | 12 |
| α-helix | 892-899 | 8 | |
| α-helix | 906-908 | 3 | |
| β-strand | 910 | 1 | 12 |
Chain Y: 15 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 663-666 | 4 | 15 |
| α-helix | 675-684 | 10 | |
| β-strand | 688-689 | 2 | 15 |
| β-strand | 697-701 | 5 | 15 |
| α-helix | 707-712 | 6 | |
| β-strand | 720-721 | 2 | 15 |
| α-helix | 723-732 | 10 | |
| α-helix | 736-738 | 3 | |
| α-helix | 740-742 | 3 | |
| β-strand | 743-745 | 3 | 15 |
| α-helix | 748-757 | 10 | |
| β-strand | 758 | 1 | 16 |
| β-strand | 764 | 1 | 16 |
| α-helix | 771-780 | 10 | |
| α-helix | 782-783 | 2 | |
| α-helix | 789-802 | 14 | |
| α-helix | 805-807 | 3 | |
| α-helix | 809-811 | 3 | |
| β-strand | 817-820 | 4 | 17 |
| β-strand | 823 | 1 | 18 |
| β-strand | 832 | 1 | 18 |
| α-helix | 837-847 | 11 | |
| β-strand | 851-853 | 3 | 17 |
| β-strand | 862-865 | 4 | 17 |
| α-helix | 872-881 | 10 | |
| β-strand | 887-890 | 4 | 17 |
| α-helix | 892-899 | 8 | |
| α-helix | 906-908 | 3 | |
| β-strand | 910 | 1 | 17 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| DNA repair protein XRCC4 | A, B, C, D | protein | 203 | Homo sapiens | Q13426 (AlphaFold model) |
| DNA ligase 4 | X, Y | protein | 263 | Homo sapiens | P49917 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>3II6_1 DNA repair protein XRCC4 (chains A, B, C, D)
MERKISRIHLVSEPSITHFLQVSWEKTLESGFVITLTDGHSAWTGTVSESEISQEADDME
MEKGKYVGELRKALLSGAGPADVYTFNFSKESCYFFFEKNLKDVSFRLGSFNLEKVENPA
EVIRELICYCLDTTAENQAKNEHLQKENERLLRDWNDVQGRFEKCVSAKEALETDLYKRF
ILVLNEKKTKIRSLHNKLLNAAQ
Sequence of entity 2 (X, Y), FASTA
>3II6_2 DNA ligase 4 (chains X, Y)
GAMGSKISNIFEDVEFCVMSGTDSQPKPDLENRIAEFGGYIVQNPGPDTYCVIAGSENIR
VKNIILSNKHDVVKPAWLLECFKTKSFVPWQPRFMIHMCPSTKEHFAREYDCYGDSYFID
TDLNQLKEVFSGIKNSNEQTPEEMASLIADLEYRYSWDCSPLSMFRRHTVYLDSYAVIND
LSTKNEGTRLAIKALELRFHGAKVVSCLAEGVSHVIIGEDHSRVADFKAFRRTFKRKFKI
LKESWVTDSIDKCELQEENQYLI
Primary citation
Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4. Wu, P.Y., Frit, P., Meesala, S. et al. Mol Cell Biol (2009) 11:3163-3172. PubMed
Other PDB entries of the same protein (UniProt Q13426 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5E50 1.38 Å, APLF/XRCC4 complex
- 7M3P 2.0 Å, Xrcc4-Spc110p(164-207) fusion
- 3MUD 2.2 Å, Structure of the Tropomyosin Overlap Complex from Chicken Smooth Muscle
- 1IK9 2.3 Å, Crystal structure of a XRCC4-DNA ligase IV complex
- 5CHX 2.3 Å, Crystal Structure of amino acids 1590-1657 of MYH7
- 5CJ0 2.3 Å, Crystal Structure of Amino Acids 1631-1692 of MYH7
- 4XA4 2.33 Å, Crystal Structure of the coiled-coil surrounding Skip 3 of MYH7
- 5WJ7 2.5 Å, Crystal Structure of Amino Acids 1733-1797 of Human Beta Cardiac Myosin Fused to Xrcc4
- 6ABO 2.65 Å, human XRCC4 and IFFO1 complex
- 1FU1 2.7 Å, Crystal structure of human XRCC4
- 9CQ3 2.8 Å, The gap-filling complex with Pol mu engaged in the NHEJ pathway
- 9N81 2.8 Å, A gap-filling complex with Pol mu engaged in the NHEJ Pathway
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