Research workbench
Ternary complex of sap-1 and srf with specific sre DNA
Analyse Ternary complex of sap-1 and srf with specific sre DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HBX
- Type
- protein + DNA
- Length
- 673 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum response factor; 5'-D(*GP*AP*TP*GP*GP*CP*CP*TP*AP*AP*TP*TP*AP*…
- UniProt
- P11831, P28324
- Pockets
- 14 · best druggability 0.69
Structure
x-ray diffraction · 7 distinct chains · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serum response factor | protein | 87 | 51% helix, 14% strand | P11831 |
| B, D | Serum response factor | protein | 86 | 51% helix, 15% strand | P11831 |
| C, F | 5'-D(*GP*AP*TP*GP*GP*CP*CP*TP*AP*AP*TP*TP*AP* GP*GP*AP*CP*TP*TP*CP*CP*GP*GP*TP*G)-3' | dna | 26 | — | — |
| E | Serum response factor | protein | 89 | 49% helix, 15% strand | P11831 |
| G | Ets-domain protein elk-4 | protein | 112 | 40% helix, 16% strand | P28324 |
| H | Ets-domain protein elk-4 | protein | 109 | 32% helix, 14% strand | P28324 |
| W, X | 5'-D(*CP*AP*CP*AP*CP*CP*GP*GP*AP*AP*GP*TP*CP* CP*TP*AP*AP*TP*TP*AP*GP*GP*CP*CP*AP*T)-3' | dna | 26 | — | — |
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 385 | 0.69 | 0.82 | 44 | empty |
| 2 | 337 | 0.68 | 0.82 | 37 | empty |
| 3 | 164 | 0.59 | 0.83 | 19 | empty |
| 4 | 206 | 0.58 | 0.80 | 28 | empty |
| 5 | 397 | 0.57 | 0.74 | 33 | empty |
Interfaces
23 interfaces between chains.
- A–B · 2024 Ų buried · 19 hydrogen bonds · protein-protein
- D–E · 1984 Ų buried · 20 hydrogen bonds · protein-protein
- C–W · 1091 Ų buried · 94 hydrogen bonds · nucleic-nucleic
- F–X · 1074 Ų buried · 84 hydrogen bonds · nucleic-nucleic
- B–G · 852 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P11831
- Every structure of UniProt P28324
- Elsewhere: RCSB PDB 1HBX · PDBe 1HBX · UniProt P11831 · UniProt P28324
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