Research workbench
Crystal structure of the mafa homodimer bound to the consensus mare
Analyse Crystal structure of the mafa homodimer bound to the consensus mare in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EOT
- Type
- protein + DNA
- Length
- 222 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription factor mafa; 5'-D(*CP*CP*GP*GP*TP*GP*CP*TP*GP*AP*GP*TP*CP*AP*GP*CP*AP*GP…
- UniProt
- Q8NHW3
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 4 distinct chains · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription factor mafa | protein | 92 | 88% helix, 0% strand | Q8NHW3 |
| B | Transcription factor mafa | protein | 92 | 88% helix, 0% strand | Q8NHW3 |
| C | 5'-D(*CP*CP*GP*GP*TP*GP*CP*TP*GP*AP*GP*TP*CP*AP*GP*CP*AP*GP *G)-3' | dna | 19 | — | — |
| D | 5'-D(*CP*CP*CP*TP*GP*CP*TP*GP*AP*CP*TP*CP*AP*GP*CP*AP*CP*CP *G)-3' | dna | 19 | — | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.56 | 0.77 | 27 | SO4 |
| 2 | 111 | 0.44 | 0.77 | 18 | empty |
| 3 | 126 | 0.43 | 0.77 | 20 | empty |
| 4 | 128 | 0.39 | 0.74 | 20 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1162 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 844 Ų buried · 96 hydrogen bonds · nucleic-nucleic
- B–D · 455 Ų buried · 9 hydrogen bonds · protein-nucleic
- A–C · 393 Ų buried · 7 hydrogen bonds · protein-nucleic
- A–D · 343 Ų buried · 6 hydrogen bonds · protein-nucleic
Compared structures
- 4EOT · Crystal structure of the MafA homodimer bound to the consensus MARE · the same entry in another collection · chain A against A, TM-score 1.00
- Q8NHW3 · AlphaFold monomer V2.0 prediction for transcription factor mafa (Q8NHW3) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 Q8NHW3
- Elsewhere: RCSB PDB 4EOT · PDBe 4EOT · UniProt Q8NHW3
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