Research workbench
Zinc uptake regulator complexed with zinc and DNA
Analyse Zinc uptake regulator complexed with zinc and DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MTE
- Type
- protein + DNA
- Length
- 664 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zinc uptake regulation protein; Znuabc operator DNA
- UniProt
- P0AC51
- Ligands
- ZN
- Pockets
- 14 · best druggability 0.62
Structure
x-ray diffraction · 6 distinct chains · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc uptake regulation protein | protein | 149 | 45% helix, 20% strand | P0AC51 |
| B | Zinc uptake regulation protein | protein | 150 | 45% helix, 21% strand | P0AC51 |
| C | Zinc uptake regulation protein | protein | 148 | 49% helix, 22% strand | P0AC51 |
| D | Zinc uptake regulation protein | protein | 151 | 43% helix, 22% strand | P0AC51 |
| Y | Znuabc operator DNA | dna | 33 | — | — |
| Z | Znuabc operator DNA | dna | 33 | — | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 500 | 0.62 | 0.76 | 57 | empty |
| 2 | 415 | 0.60 | 0.76 | 49 | empty |
| 3 | 273 | 0.59 | 0.79 | 30 | empty |
| 4 | 192 | 0.54 | 0.79 | 31 | empty |
| 5 | 54 | 0.53 | 0.89 | 20 | empty |
Interfaces
12 interfaces between chains.
- A–D · 1429 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1393 Ų buried · 17 hydrogen bonds · protein-protein
- Y–Z · 1392 Ų buried · 144 hydrogen bonds · nucleic-nucleic
- B–Y · 473 Ų buried · 8 hydrogen bonds · protein-nucleic
- D–Y · 464 Ų buried · 7 hydrogen bonds · protein-nucleic
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 P0AC51
- Elsewhere: RCSB PDB 4MTE · PDBe 4MTE · UniProt P0AC51
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