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Crystal structure of dimerized N-terminal domain of minc
Analyse Crystal structure of dimerized N-terminal domain of minc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L1C
- Type
- protein
- Length
- 196 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable septum site-determining protein minc
- UniProt
- Q1RCS1
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Probable septum site-determining protein minc | protein | 98 | 36% helix, 30% strand | Q1RCS1 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.36 | 0.74 | 20 | empty |
| 2 | 69 | 0.29 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1768 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 4L1C · Crystal structure of Dimerized N-terminal Domain of MinC · the same entry in another collection · chain A against A, 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 Q1RCS1
- Elsewhere: RCSB PDB 4L1C · PDBe 4L1C · UniProt Q1RCS1
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