3KJL: Sgf11:Sus1 complex
Sgf11:Sus1 complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 8 Dec 2009.
- Method
- X-ray diffraction
- Resolution
- 2.7 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 8
- Atoms
- 3,647
- Mol. weight
- 58.39 kDa
- Released
- 8 Dec 2009
Explore 3KJL in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3KJL contains 20 α-helices and 0 β-strands across 8 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: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-35 | 27 | |
| α-helix | 38-52 | 15 | |
| α-helix | 58-72 | 15 | |
| α-helix | 75-91 | 17 | |
Chain B: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-35 | 14 | |
| α-helix | 38-52 | 15 | |
| α-helix | 58-72 | 15 | |
| α-helix | 75-93 | 19 | |
Chain C: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-36 | 15 | |
| α-helix | 38-52 | 15 | |
| α-helix | 58-72 | 15 | |
| α-helix | 75-90 | 16 | |
Chain D: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-36 | 25 | |
| α-helix | 38-52 | 15 | |
| α-helix | 58-72 | 15 | |
| α-helix | 75-87 | 13 | |
Chain E: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-31 | 26 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-28 | 22 | |
Chain G: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-31 | 20 | |
Chain H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-31 | 29 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein SUS1 | A, B, C, D | protein | 96 | Saccharomyces cerevisiae | Q6WNK7 (AlphaFold model) |
| SAGA-associated factor 11 | E, F, G, H | protein | 32 | Saccharomyces cerevisiae | Q03067 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>3KJL_1 Protein SUS1 (chains A, B, C, D)
MTMDTAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDLTKSEMNINESTNFTQ
ILSTVEPKALEMVSDSTRETVLKQIREFLEEIVDTQ
Sequence of entity 2 (E, F, G, H), FASTA
>3KJL_2 SAGA-associated factor 11 (chains E, F, G, H)
TEETITIDSISNGILNNLLTTLIQDIVARETT
Primary citation
Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1. Ellisdon, A.M., Jani, D., Kohler, A. et al. J Biol Chem (2010) 285:3850-3856. DOI 10.1074/jbc.M109.070839 · PubMed
Other PDB entries of the same protein (UniProt Q6WNK7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3MHS 1.89 Å, Structure of the SAGA Ubp8/Sgf11/Sus1/Sgf73 DUB module bound to ubiquitin aldehyde
- 4FK5 2.03 Å, Structure of the SAGA Ubp8(S144N)/Sgf11/Sus1/Sgf73 DUB module
- 3KIK 2.1 Å, Sgf11:Sus1 complex
- 6AQR 2.1 Å, SAGA DUB module Ubp8(C146A)/Sgf11/Sus1/Sgf73 bound to monoubiquitin
- 4WA6 2.36 Å, Structure of yeast SAGA DUBm with Sgf73 N59D mutant at 2.36 angstroms resolution
- 3MHH 2.45 Å, Structure of the SAGA Ubp8/Sgf11/Sus1/Sgf73 DUB module
- 3FWB 2.5 Å, Sac3:Sus1:Cdc31 complex
- 4MBE 2.61 Å, Sac3:Sus1:Cdc31:Nup1 complex
- 4FIP 2.69 Å, Structure of the SAGA Ubp8(S144N)/Sgf11(1-72, Delta-ZnF)/Sus1/Sgf73 DUB module
- 3FWC 2.7 Å, Sac3:Sus1:Cdc31 complex
- 3M99 2.7 Å, Structure of the Ubp8-Sgf11-Sgf73-Sus1 SAGA DUB module
- 4FJC 2.83 Å, Structure of the SAGA Ubp8/Sgf11(1-72, Delta-ZnF)/Sus1/Sgf73 DUB module
Browse structure collections
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