Research workbench
Maltose binding-A1 homeodomain protein chimera, crystal form II
Analyse Maltose binding-A1 homeodomain protein chimera, crystal form II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MH4
- Type
- protein
- Length
- 418 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose binding-A1 homeodomain protein chimera
- UniProt
- P02928, P01366
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose binding-A1 homeodomain protein chimera | protein | 418 | 48% helix, 18% strand | P02928, P01366 |
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 | 577 | 0.77 | 0.83 | 65 | empty |
| 2 | 53 | 0.36 | 0.79 | 14 | empty |
| 3 | 52 | 0.27 | 0.74 | 15 | empty |
Compared structures
- 1MH4 · maltose binding-a1 homeodomain protein chimera, crystal form II · 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 P02928
- Every structure of UniProt P01366
- Elsewhere: RCSB PDB 1MH4 · PDBe 1MH4 · UniProt P02928 · UniProt P01366
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