3RL7: HDLG1-PDZ1
Crystal structure of hDLG1-PDZ1 complexed with APC. Determined by X-ray diffraction at 2.3 Å resolution. Released 14 Dec 2011.
- Method
- X-ray diffraction
- Resolution
- 2.3 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 4,352
- Mol. weight
- 78.44 kDa
- Released
- 14 Dec 2011
Explore 3RL7 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3RL7 contains 15 α-helices and 54 β-strands across 12 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: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 222-228 | 7 | 3 |
| β-strand | 230 | 1 | 4 |
| β-strand | 233 | 1 | 4 |
| β-strand | 236-239 | 4 | 3 |
| β-strand | 254-258 | 5 | 3 |
| α-helix | 263-267 | 5 | |
| β-strand | 275-279 | 5 | 3 |
| β-strand | 282-283 | 2 | 3 |
| α-helix | 289-297 | 9 | |
| β-strand | 302-308 | 7 | 3 |
Chains B and D: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 221-228 | 8 | 1 |
| β-strand | 230 | 1 | 2 |
| β-strand | 233 | 1 | 2 |
| β-strand | 236-239 | 4 | 1 |
| β-strand | 254-258 | 5 | 1 |
| α-helix | 263-267 | 5 | |
| α-helix | 274 | 1 | |
| β-strand | 275-279 | 5 | 1 |
| β-strand | 282-283 | 2 | 1 |
| α-helix | 289-298 | 10 | |
| β-strand | 302-309 | 8 | 1 |
Chain C: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 221-228 | 8 | 5 |
| β-strand | 230 | 1 | 6 |
| β-strand | 233 | 1 | 6 |
| β-strand | 236-239 | 4 | 5 |
| β-strand | 253-258 | 6 | 5 |
| α-helix | 263-267 | 5 | |
| β-strand | 275-279 | 5 | 5 |
| β-strand | 282-283 | 2 | 5 |
| α-helix | 289-297 | 9 | |
| β-strand | 302-309 | 8 | 5 |
Chain E: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 221-228 | 8 | 9 |
| β-strand | 230 | 1 | 10 |
| β-strand | 233 | 1 | 10 |
| β-strand | 236-239 | 4 | 9 |
| β-strand | 253-258 | 6 | 9 |
| α-helix | 263-267 | 5 | |
| β-strand | 275-279 | 5 | 9 |
| β-strand | 282-283 | 2 | 9 |
| α-helix | 289-298 | 10 | |
| β-strand | 302-309 | 8 | 9 |
Chain F: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 222-228 | 7 | 11 |
| β-strand | 230 | 1 | 12 |
| β-strand | 233 | 1 | 12 |
| β-strand | 236-239 | 4 | 11 |
| β-strand | 253-258 | 6 | 11 |
| α-helix | 263-267 | 5 | |
| α-helix | 274 | 1 | |
| β-strand | 275-279 | 5 | 11 |
| β-strand | 282-283 | 2 | 11 |
| α-helix | 289-298 | 10 | |
| β-strand | 302-308 | 7 | 11 |
Chain G: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2840-2842 | 3 | 3 |
Chain H: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2840-2841 | 2 | 1 |
Chains I and L: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2841 | 1 | 7 |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Disks large homolog 1 | A, B, C, D, E, F | protein | 107 | Homo sapiens | Q12959 (AlphaFold model) |
| 11-mer peptide from Adenomatous polyposis coli protein | G, H, I, J, K, L | protein | 11 | Homo sapiens | P25054 |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>3RL7_1 Disks large homolog 1 (chains A, B, C, D, E, F)
MGHHHHHHMYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRL
RVNDCILRVNEVDVRDVTHSKAVEALKEAGSIVRLYVKRRKPVSEKI
Sequence of entity 2 (G, H, I, J, K, L), FASTA
>3RL7_2 11-mer peptide from Adenomatous polyposis coli protein (chains G, H, I, J, K, L)
RHSGSYLVTSV
Primary citation
Molecular basis for the recognition of adenomatous polyposis coli by the Discs Large 1 protein. Zhang, Z., Li, H., Chen, L. et al. PLoS One (2011) 6:e23507-e23507. DOI 10.1371/journal.pone.0023507 · PubMed
Other PDB entries of the same protein (UniProt Q12959 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7PC3 1.95 Å, The second PDZ domain of DLG1 complexed with the PDZ-binding motif of HTLV1-TAX1
- 2X7Z 2.0 Å, Crystal Structure of the SAP97 PDZ2 I342W C378A mutant protein domain
- 4G69 2.0 Å, Structure of the Human Discs Large 1 PDZ2 - Adenomatous Polyposis Coli Cytoskeletal…
- 8CN1 2.09 Å, hDLG1-PDZ1 in complex with a TAX1 peptide from HTLV-1
- 3RL8 2.2 Å, Crystal structure of hDLG1-PDZ2 complexed with APC
- 3W9Y 2.2 Å, Crystal structure of the human DLG1 guanylate kinase domain
- 4AMH 2.3 Å, Influence of circular permutation on the folding pathway of a PDZ domain
- 8CN3 2.71 Å, hDLG1-PDZ2 in complex with a TAX1 peptide from HTLV-1
- 1PDR 2.8 Å, Crystal structure of the third PDZ domain from the human homolog of discs large protein
- 3LRA 2.95 Å, Structural Basis for Assembling a Human Tripartite Complex Dlg1-MPP7-Mals3
- 2M3M Solution structure of a complex consisting of hDlg/SAP-97 residues 318-406 and HPV51…
- 2OQS Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide
Browse structure collections
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