Research workbench
Methanol dehydrogenase from methylacidiphilum fumariolicum solv
Analyse Methanol dehydrogenase from methylacidiphilum fumariolicum solv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MAE
- Type
- protein
- Length
- 1,154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methanol dehydrogenase
- EC
- 1.1.2.7, 1.1.2.8
- UniProt
- I0JWN7
- Ligands
- PQQ, CE
- Pockets
- 8 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Methanol dehydrogenase (EC 1.1.2.7, 1.1.2.8) | protein | 577 | 11% helix, 36% strand | I0JWN7 |
Ligands and binding sites
- PQQ · Pyrroloquinoline quinone · ligand · 2 copies · chains A, B
- CE · Cerium (III) ion · metal · 2 copies · chains A, B
- 15P · Polyethylene glycol (N=34) · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.66 | 0.86 | 38 | PQQ, 15P |
| 2 | 171 | 0.66 | 0.86 | 42 | PQQ, 15P |
| 3 | 200 | 0.52 | 0.77 | 25 | empty |
| 4 | 193 | 0.49 | 0.76 | 25 | empty |
| 5 | 158 | 0.46 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1192 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4MAE · Methanol dehydrogenase from Methylacidiphilum fumariolicum SolV · 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 I0JWN7
- Elsewhere: RCSB PDB 4MAE · PDBe 4MAE · UniProt I0JWN7
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