Mutagenesis of tryptophan199 reveals that electron hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis
Jensen, L.M.R., Wilmot, C.M.To be published.
Experimental Data Snapshot
Starting Model: experimental
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Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Methylamine utilization protein MauG | 373 | Paracoccus denitrificans PD1222 | Mutation(s): 1 Gene Names: mauG, Pden_4736 EC: 1 | ![]() | |
UniProt | |||||
Find proteins for Q51658 (Paracoccus denitrificans (strain Pd 1222)) Explore Q51658 Go to UniProtKB: Q51658 | |||||
Entity Groups | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q51658 | ||||
Sequence AnnotationsExpand | |||||
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Entity ID: 2 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Methylamine dehydrogenase light chain | 137 | Paracoccus denitrificans PD1222 | Mutation(s): 0 Gene Names: Pden_4733 EC: 1.4.99.3 (PDB Primary Data), 1.4.9.1 (UniProt) | ![]() | |
UniProt | |||||
Find proteins for A1BBA0 (Paracoccus denitrificans (strain Pd 1222)) Explore A1BBA0 Go to UniProtKB: A1BBA0 | |||||
Entity Groups | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | A1BBA0 | ||||
Sequence AnnotationsExpand | |||||
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Entity ID: 3 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Methylamine dehydrogenase heavy chain | 386 | Paracoccus denitrificans PD1222 | Mutation(s): 0 Gene Names: Pden_4730 EC: 1.4.99.3 (PDB Primary Data), 1.4.9.1 (UniProt) | ![]() | |
UniProt | |||||
Find proteins for A1BB97 (Paracoccus denitrificans (strain Pd 1222)) Explore A1BB97 Go to UniProtKB: A1BB97 | |||||
Entity Groups | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | A1BB97 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 7 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
HEC Query on HEC | J [auth A], K [auth A], O [auth B], P [auth B] | HEME C C34 H34 Fe N4 O4 HXQIYSLZKNYNMH-LJNAALQVSA-N | |||
1PE Query on 1PE | R [auth F] | PENTAETHYLENE GLYCOL C10 H22 O6 JLFNLZLINWHATN-UHFFFAOYSA-N | |||
PG4 Query on PG4 | S [auth F] | TETRAETHYLENE GLYCOL C8 H18 O5 UWHCKJMYHZGTIT-UHFFFAOYSA-N | |||
EDO Query on EDO | Q [auth B] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N | |||
ACT Query on ACT | T [auth F] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M | |||
CA Query on CA | G [auth A], L [auth B] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N | |||
NA Query on NA | H [auth A], I [auth A], M [auth B], N [auth B] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |
Modified Residues 1 Unique | |||||
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ID | Chains | Type | Formula | 2D Diagram | Parent |
0AF Query on 0AF | C, E | L-PEPTIDE LINKING | C11 H12 N2 O3 | TRP |
Length ( Å ) | Angle ( ˚ ) |
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a = 55.527 | α = 109.94 |
b = 83.524 | β = 91.54 |
c = 107.782 | γ = 105.78 |
Software Name | Purpose |
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Blu-Ice | data collection |
REFMAC | refinement |
HKL-2000 | data reduction |
HKL-2000 | data scaling |
REFMAC | phasing |