Research workbench
Structure of bacteriophage lambda cii protein in complex with DNA
Analyse Structure of bacteriophage lambda cii protein in complex with DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZS4
- Type
- protein + DNA
- Length
- 370 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA - 27MER; Regulatory protein cii
- UniProt
- P03042
- Pockets
- 7 · best druggability 0.53
Structure
x-ray diffraction · 5 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| U | DNA - 27MER | dna | 27 | — | — |
| T | DNA - 27MER | dna | 27 | — | — |
| A, B | Regulatory protein cii | protein | 82 | 76% helix, 0% strand | P03042 |
| C | Regulatory protein cii | protein | 79 | 80% helix, 0% strand | P03042 |
| D | Regulatory protein cii | protein | 73 | 81% helix, 0% strand | P03042 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.53 | 0.76 | 25 | empty |
| 2 | 144 | 0.48 | 0.78 | 22 | empty |
| 3 | 157 | 0.47 | 0.77 | 16 | empty |
| 4 | 158 | 0.43 | 0.74 | 23 | empty |
| 5 | 87 | 0.41 | 0.78 | 20 | empty |
Interfaces
15 interfaces between chains.
- A–B · 1471 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 1460 Ų buried · 5 hydrogen bonds · protein-protein
- U–T · 1172 Ų buried · 92 hydrogen bonds · nucleic-nucleic
- B–C · 810 Ų buried · 15 hydrogen bonds · protein-protein
- U–C · 382 Ų buried · 6 hydrogen bonds · protein-nucleic
Compared structures
- 1ZS4 · Structure of bacteriophage lambda cII protein in complex with DNA · the same entry in another collection · chain U against U, 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 P03042
- Elsewhere: RCSB PDB 1ZS4 · PDBe 1ZS4 · UniProt P03042
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