Activity regulation of the aminodeoxychorismate synthase bienzyme complex by glutaminase substrate-mediated subunit interface expansion
Sung, S., Funke, F.J., Schlee, S., Sterner, R., Wilmanns, 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 |
Aminodeoxychorismate synthase component 2 | A [auth AAA], B [auth BBB] | 189 | Escherichia coli | Mutation(s): 0  Gene Names: pabA, b3360, JW3323 EC: 2.6.1.85 | |
UniProt | |||||
Find proteins for P00903 (Escherichia coli (strain K12)) Explore P00903  Go to UniProtKB:  P00903 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P00903 | ||||
Sequence AnnotationsExpand | |||||
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Entity ID: 2 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Aminodeoxychorismate synthase component 1 | C [auth CCC], D [auth DDD] | 455 | Escherichia coli | Mutation(s): 0  Gene Names: pabB, b1812, JW1801 EC: 2.6.1.85 | |
UniProt | |||||
Find proteins for P05041 (Escherichia coli (strain K12)) Explore P05041  Go to UniProtKB:  P05041 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P05041 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 7 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
ISJ (Subject of Investigation/LOI) Query on ISJ | I [auth CCC], U [auth DDD] | (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid C10 H10 O6 WTFXTQVDAKGDEY-HTQZYQBOSA-N | |||
TRP (Subject of Investigation/LOI) Query on TRP | J [auth CCC], V [auth DDD] | TRYPTOPHAN C11 H12 N2 O2 QIVBCDIJIAJPQS-VIFPVBQESA-N | |||
GLU (Subject of Investigation/LOI) Query on GLU | E [auth AAA] | GLUTAMIC ACID C5 H9 N O4 WHUUTDBJXJRKMK-VKHMYHEASA-N | |||
SO4 Query on SO4 | CA [auth DDD], DA [auth DDD], G [auth AAA], H [auth BBB], T [auth CCC] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L | |||
GOL Query on GOL | AA [auth DDD] BA [auth DDD] F [auth AAA] Q [auth CCC] R [auth CCC] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N | |||
CL Query on CL | L [auth CCC] M [auth CCC] N [auth CCC] O [auth CCC] P [auth CCC] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M | |||
MG (Subject of Investigation/LOI) Query on MG | K [auth CCC], W [auth DDD], X [auth DDD] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |
Length ( Å ) | Angle ( ˚ ) |
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a = 80.184 | α = 90 |
b = 109.946 | β = 90 |
c = 175.619 | γ = 90 |
Software Name | Purpose |
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REFMAC | refinement |
XDS | data reduction |
Aimless | data scaling |
PHASER | phasing |
Funding Organization | Location | Grant Number |
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H2020 Marie Curie Actions of the European Commission | European Union | 664726 |