Research workbench
Crystal structure of the W199F-MAUG/PRE-methylamine dehydrogenase complex
Analyse Crystal structure of the W199F-MAUG/PRE-methylamine dehydrogenase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RMZ
- Type
- protein
- Length
- 1,716 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q51658, A1BBA0, A1BB97
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 354 | — | Q51658 |
| B | — | protein | 355 | — | Q51658 |
| C | — | protein | 131 | — | A1BBA0 |
| D, F | — | protein | 376 | — | A1BB97 |
| E | — | protein | 124 | — | A1BBA0 |
Compared structures
- 3RMZ · Crystal Structure of the W199F-MauG/pre-Methylamine Dehydrogenase Complex · the same entry in another collection · chain F against F, TM-score 1.00
- Q51658 · AlphaFold monomer V2.0 prediction for methylamine utilization protein maug (Q51658) · a predicted model of the same protein · chain B 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 Q51658
- Every structure of UniProt A1BBA0
- Every structure of UniProt A1BB97
- Elsewhere: RCSB PDB 3RMZ · PDBe 3RMZ · UniProt Q51658 · UniProt A1BBA0 · UniProt A1BB97
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