MolNFT v1 · #101783 · protein
Crystal structure of the Q103N-MAUG/PRE-methylamine dehydrogenase complex
4O1Q · Methylamine utilization protein maug: “Crystal structure of the Q103N-MAUG/PRE-methylamine dehydrogenase complex”. X-ray diffraction, 4 ligands (HEC, CA, NA), 20 pockets (best druggability 0.86). MolNFT v1 #101783 on GenesisL1: 3D…
- PDB
- 4O1Q
- Type
- protein
- Length
- 1,711 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, CA, NA, PO4
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 27% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methylamine utilization protein maug (EC 1.-.-.-) | protein | 354 | 41% helix, 8% strand | Q51658 |
| B | Methylamine utilization protein maug (EC 1.-.-.-) | protein | 355 | 41% helix, 7% strand | Q51658 |
| C, E | Methylamine dehydrogenase light chain (EC 1.4.99.3) | protein | 125 | 10% helix, 32% strand | A1BBA0 |
| D, F | Methylamine dehydrogenase heavy chain (EC 1.4.99.3) | protein | 376 | 7% helix, 47% strand | A1BB97 |
Ligands and binding sites
- HEC · Heme C · ligand · 4 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
- NA · Sodium ion · metal · chains F
- PO4 · Phosphate ion · ion · chains B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains D, F
- PGE · Triethylene glycol · additive · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 621 | 0.86 | 0.91 | 89 | CA, HEC |
| 2 | 601 | 0.86 | 0.90 | 83 | CA, HEC |
| 3 | 223 | 0.82 | 0.95 | 40 | empty |
| 4 | 226 | 0.81 | 0.94 | 38 | empty |
| 5 | 992 | 0.77 | 0.79 | 105 | empty |
Interfaces
11 interfaces between chains.
- C–D · 1695 Ų buried · 36 hydrogen bonds · protein-protein
- E–F · 1693 Ų buried · 29 hydrogen bonds · protein-protein
- D–E · 1357 Ų buried · 25 hydrogen bonds · protein-protein
- C–F · 1336 Ų buried · 25 hydrogen bonds · protein-protein
- B–E · 868 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide, 8 cofactor, 2 modified (disulfide, heme c attachment, nonstandard).
Compared structures
- 4O1Q · Crystal Structure of the Q103N-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 4O1Q · PDBe 4O1Q · UniProt Q51658 · UniProt A1BBA0 · UniProt A1BB97
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