MolNFT v1 · #74272 · protein
Crystal structure of the Y294H-MAUG/PRE-methylamine dehydrogenase complex
3ORV · Methylamine utilization protein maug: “Crystal structure of the Y294H-MAUG/PRE-methylamine dehydrogenase complex”. X-ray diffraction, 2 ligands (HEC, CA), 19 pockets (best druggability 0.87). MolNFT v1 #74272 on GenesisL1: 3D…
- PDB
- 3ORV
- Type
- protein
- Length
- 1,709 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, P22619, A1BB97
- Ligands
- HEC, CA
- Pockets
- 19 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 28% helix, 22% 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 | 355 | 41% helix, 8% strand | Q51658 |
| C, E | Methylamine dehydrogenase light chain (EC 1.4.99.3) | protein | 124 | 10% helix, 32% strand | P22619 |
| 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
- EDO · 1,2-ethanediol · additive · 3 copies · chains B, D, F
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains C, D, E, F
- PG4 · Tetraethylene glycol · additive · 2 copies · chains F, D
- PGE · Triethylene glycol · additive · chains D
- P6G · Hexaethylene glycol · additive · chains F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 676 | 0.87 | 0.91 | 93 | HEC |
| 2 | 703 | 0.87 | 0.91 | 94 | CA, HEC |
| 3 | 243 | 0.81 | 0.93 | 38 | EDO |
| 4 | 245 | 0.80 | 0.92 | 39 | PEG |
| 5 | 981 | 0.78 | 0.80 | 102 | PEG |
Interfaces
11 interfaces between chains.
- E–F · 1688 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 1669 Ų buried · 28 hydrogen bonds · protein-protein
- C–F · 1340 Ų buried · 19 hydrogen bonds · protein-protein
- D–E · 1306 Ų buried · 18 hydrogen bonds · protein-protein
- B–E · 808 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 8 cofactor, 2 modified (disulfide, heme c attachment, nonstandard).
Compared structures
- 3ORV · Crystal Structure of the Y294H-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
- P22619 · AlphaFold monomer V2.0 prediction for methylamine dehydrogenase light chain (P22619) · a predicted model of the same protein · chain E against A, TM-score 0.99
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 P22619
- Every structure of UniProt A1BB97
- Elsewhere: RCSB PDB 3ORV · PDBe 3ORV · UniProt Q51658 · UniProt P22619 · UniProt A1BB97
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