Crystal structure of yeast N-terminal acetyltransferase NatE (ppGpp) in complex with a bisubstrate
Dong, J., Wang, S., York, J.D.To be published.
Experimental Data Snapshot
Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
N-terminal acetyltransferase A complex subunit NAT1 | 854 | Saccharomyces cerevisiae | Mutation(s): 0  | ||
UniProt | |||||
Find proteins for P12945 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P12945  Go to UniProtKB:  P12945 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P12945 | ||||
Sequence AnnotationsExpand | |||||
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Entity ID: 2 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
N-terminal acetyltransferase A complex catalytic subunit ARD1 | 238 | Saccharomyces cerevisiae | Mutation(s): 0  EC: 2.3.1.88 (PDB Primary Data), 2.3.1.255 (UniProt) | ||
UniProt | |||||
Find proteins for P07347 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P07347  Go to UniProtKB:  P07347 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P07347 | ||||
Sequence AnnotationsExpand | |||||
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Entity ID: 3 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
N-terminal acetyltransferase A complex subunit NAT5 | 176 | Saccharomyces cerevisiae | Mutation(s): 0  EC: 2.3.1 (PDB Primary Data), 2.3.1.258 (UniProt) | ||
UniProt | |||||
Find proteins for Q08689 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore Q08689  Go to UniProtKB:  Q08689 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q08689 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by: Sequence | 3D Structure
Entity ID: 4 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
human ACTH8 | D [auth F] | 8 | Homo sapiens | Mutation(s): 0  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01189 (Homo sapiens) Explore P01189  Go to UniProtKB:  P01189 | |||||
PHAROS:  P01189 GTEx:  ENSG00000115138  | |||||
Entity Groups   | |||||
UniProt Group | P01189 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 3 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
CMC Query on CMC | G [auth F] | CARBOXYMETHYL COENZYME *A C23 H38 N7 O18 P3 S OBUOSIHPWVNVJN-GRFIIANRSA-N | |||
ACO Query on ACO | F [auth C] | ACETYL COENZYME *A C23 H38 N7 O17 P3 S ZSLZBFCDCINBPY-ZSJPKINUSA-N | |||
G4P Query on G4P | E [auth A] | GUANOSINE-5',3'-TETRAPHOSPHATE C10 H17 N5 O17 P4 BUFLLCUFNHESEH-UUOKFMHZSA-N |
Length ( ? ) | Angle ( ? ) |
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a = 85.564 | ¦Á = 90 |
b = 113.649 | ¦Â = 90 |
c = 146.721 | ¦Ă = 90 |
Software Name | Purpose |
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REFMAC | refinement |
HKL-2000 | data reduction |
HKL-2000 | data scaling |
PHASER | phasing |