Research workbench
Crystal structure of the E113Q-MAUG/PRE-methylamine dehydrogenase complex
Analyse Crystal structure of the E113Q-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
- 4L1Q
- Type
- protein
- Length
- 1,719 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methylamine utilization protein maug; Methylamine dehydrogenase light chain; Methylamine…
- EC
- 1.-.-.-, 1.4.99.3
- UniProt
- Q51658, A1BBA0, A1BB97
- Ligands
- HEC, NA, CA
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 5 distinct chains · 27% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methylamine utilization protein maug (EC 1.-.-.-) | protein | 354 | 42% helix, 7% strand | Q51658 |
| B | Methylamine utilization protein maug (EC 1.-.-.-) | protein | 357 | 44% helix, 7% strand | Q51658 |
| C | Methylamine dehydrogenase light chain (EC 1.4.99.3) | protein | 131 | 9% helix, 30% strand | A1BBA0 |
| D, F | Methylamine dehydrogenase heavy chain (EC 1.4.99.3) | protein | 376 | 7% helix, 48% strand | A1BB97 |
| E | Methylamine dehydrogenase light chain (EC 1.4.99.3) | protein | 125 | 10% helix, 34% strand | A1BBA0 |
Ligands and binding sites
- HEC · Heme C · ligand · 4 copies · chains A, B
- NA · Sodium ion · metal · 3 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 628 | 0.86 | 0.90 | 88 | HEC |
| 2 | 616 | 0.86 | 0.91 | 88 | CA, HEC |
| 3 | 210 | 0.80 | 0.94 | 38 | empty |
| 4 | 217 | 0.80 | 0.94 | 38 | empty |
| 5 | 1014 | 0.77 | 0.80 | 108 | empty |
Interfaces
11 interfaces between chains.
- C–D · 1702 Ų buried · 29 hydrogen bonds · protein-protein
- E–F · 1661 Ų buried · 28 hydrogen bonds · protein-protein
- D–E · 1328 Ų buried · 23 hydrogen bonds · protein-protein
- C–F · 1318 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 988 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide, 8 cofactor, 2 modified (disulfide, heme c attachment, nonstandard).
Compared structures
- 4L1Q · Crystal Structure of the E113Q-MauG/pre-Methylamine Dehydrogenase Complex · 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 Q51658
- Every structure of UniProt A1BBA0
- Every structure of UniProt A1BB97
- Elsewhere: RCSB PDB 4L1Q · PDBe 4L1Q · UniProt Q51658 · UniProt A1BBA0 · UniProt A1BB97
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.