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The crystal structure of a mutant protein with altered but improved hydrophobic core packing
Analyse The crystal structure of a mutant protein with altered but improved hydrophobic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LLI
- Type
- protein + DNA
- Length
- 221 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'- D(*AP*AP*TP*AP*CP*CP*AP*CP*TP*GP*GP*CP*GP*GP*TP*GP*A P*TP*AP*T)-3'); DNA (5'…
- UniProt
- P03034
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 4 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | DNA (5'- D(*AP*AP*TP*AP*CP*CP*AP*CP*TP*GP*GP*CP*GP*GP*TP*GP*A P*TP*AP*T)-3') | dna | 20 | — | — |
| E | DNA (5'- D(*TP*AP*TP*AP*TP*CP*AP*CP*CP*GP*CP*CP*AP*GP*TP*GP*G P*TP*AP*T)-3') | dna | 20 | — | — |
| A | Protein (lambda repressor) | protein | 89 | 70% helix, 0% strand | P03034 |
| B | Protein (lambda repressor) | protein | 92 | 65% helix, 0% strand | P03034 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.54 | 0.74 | 45 | empty |
| 2 | 69 | 0.43 | 0.81 | 16 | empty |
Interfaces
6 interfaces between chains.
- D–E · 875 Ų buried · 89 hydrogen bonds · nucleic-nucleic
- A–B · 752 Ų buried · 8 hydrogen bonds · protein-protein
- D–B · 545 Ų buried · 16 hydrogen bonds · protein-nucleic
- E–B · 495 Ų buried · 14 hydrogen bonds · protein-nucleic
- E–A · 374 Ų buried · 9 hydrogen bonds · protein-nucleic
Compared structures
- 1LLI · The crystal structure of a mutant protein with altered but improved hydrophobic core… · the same entry in another collection · chain D against D, TM-score 1.00
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 P03034
- Elsewhere: RCSB PDB 1LLI · PDBe 1LLI · UniProt P03034
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