Research workbench
Gphf DH1 P1711L, L1744P variant: an isomerase-inactive variant of gphf DH1
Analyse Gphf DH1 P1711L, L1744P variant: an isomerase-inactive variant of gphf DH1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MBH
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gphf dehydratase 1
- UniProt
- U6BSB2
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gphf dehydratase 1 | protein | 286 | 20% helix, 41% strand | U6BSB2 |
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 | 160 | 0.67 | 0.87 | 35 | empty |
| 2 | 82 | 0.32 | 0.74 | 18 | empty |
Compared structures
- 6MBH · GphF DH1 P1711L, L1744P variant: An isomerase-inactive variant of GphF DH1 · 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 U6BSB2
- Elsewhere: RCSB PDB 6MBH · PDBe 6MBH · UniProt U6BSB2
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