Research workbench
Structure of MCM10 coiled-coil region
Analyse Structure of MCM10 coiled-coil region in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JBZ
- Type
- protein
- Length
- 1,201 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic protein fused with xenopus laevis MCM10 coiled-coil region
- UniProt
- P0AEX9, Q5EAW4
- Ligands
- GLC
- Pockets
- 15 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding periplasmic protein fused with xenopus laevis MCM10 coiled-coil region | protein | 401 | 48% helix, 19% strand | P0AEX9, Q5EAW4 |
| B, C | Maltose-binding periplasmic protein fused with xenopus laevis MCM10 coiled-coil region | protein | 400 | 47% helix, 19% strand | P0AEX9, Q5EAW4 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 6 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 981 | 0.78 | 0.80 | 87 | GLC |
| 2 | 1081 | 0.75 | 0.78 | 81 | GLC |
| 3 | 251 | 0.70 | 0.85 | 31 | GLC |
| 4 | 574 | 0.69 | 0.78 | 59 | empty |
| 5 | 124 | 0.46 | 0.78 | 17 | empty |
Interfaces
3 interfaces between chains.
- B–C · 787 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 729 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 715 Ų buried · 1 hydrogen bond · protein-protein
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 P0AEX9
- Every structure of UniProt Q5EAW4
- Elsewhere: RCSB PDB 4JBZ · PDBe 4JBZ · UniProt P0AEX9 · UniProt Q5EAW4
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