Research workbench
Maltose binding-A1 homeodomain protein chimera, crystal form I
Analyse Maltose binding-A1 homeodomain protein chimera, crystal form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MH3
- Type
- protein
- Length
- 421 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
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose binding-A1 homeodomain protein chimera | protein | 421 | 49% helix, 18% strand | P02928, P01366 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 669 | 0.77 | 0.82 | 74 | empty |
| 2 | 68 | 0.29 | 0.74 | 15 | empty |
Compared structures
- 1MH3 · maltose binding-a1 homeodomain protein chimera, crystal form I · 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 1MH3 · PDBe 1MH3 · UniProt P02928 · UniProt P01366
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