Research workbench
Melanoma differentiation associated protein-5 helicase domain complex with inhibitor non-structural protein V
Analyse Melanoma differentiation associated protein-5 helicase domain complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I1S
- Type
- protein
- Length
- 290 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Melanoma differentiation associated protein-5; Non-structural protein V
- UniProt
- A7LCX1, P11207
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Melanoma differentiation associated protein-5 | protein | 238 | 63% helix, 9% strand | A7LCX1 |
| B | Non-structural protein V | protein | 52 | 6% helix, 38% strand | P11207 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 221 | 0.57 | 0.79 | 35 | empty |
| 2 | 162 | 0.46 | 0.76 | 28 | empty |
| 3 | 148 | 0.43 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1129 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4I1S · Melanoma differentiation associated protein-5 Helicase domain complex with inhibitor… · 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 A7LCX1
- Every structure of UniProt P11207
- Elsewhere: RCSB PDB 4I1S · PDBe 4I1S · UniProt A7LCX1 · UniProt P11207
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