Research workbench
Structure of HPV49 E6 protein in complex with MAML1 lxxll motif
Analyse Structure of HPV49 E6 protein in complex with MAML1 lxxll motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SMV
- Type
- protein
- Length
- 525 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,PROTEIN E6,MASTERMIND-like protein 1
- UniProt
- P0AEX9, P36813, Q92585
- Ligands
- GLC, ZN
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,PROTEIN E6,MASTERMIND-like protein 1 | protein | 525 | 43% helix, 18% strand | P0AEX9, P36813, Q92585 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 385 | 0.74 | 0.85 | 36 | GLC |
| 2 | 50 | 0.71 | 0.98 | 17 | empty |
| 3 | 365 | 0.58 | 0.76 | 47 | empty |
| 4 | 50 | 0.30 | 0.76 | 15 | empty |
Compared structures
- 6SMV · Structure of HPV49 E6 protein in complex with MAML1 LxxLL motif · the same entry in another collection · chain A against A, TM-score 1.00
- Q92585 · AlphaFold monomer V2.0 prediction for mastermind-like protein 1 (Q92585) · a predicted model of the same protein · chain A against A, TM-score 0.18
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 P0AEX9
- Every structure of UniProt P36813
- Every structure of UniProt Q92585
- Elsewhere: RCSB PDB 6SMV · PDBe 6SMV · UniProt P0AEX9 · UniProt P36813 · UniProt Q92585
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