The Structure of Torpedo Californica Acetylcholinesterase Complexed with 2-Pam
Harel, M., Silman, I., Sussman, J.L.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 |
ACETYLCHOLINESTERASE | 543 | Tetronarce californica | Mutation(s): 0  EC: 3.1.1.7 | ||
UniProt | |||||
Find proteins for P04058 (Tetronarce californica) Explore P04058  Go to UniProtKB:  P04058 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P04058 | ||||
Glycosylation | |||||
Glycosylation Sites: 2 | |||||
Sequence AnnotationsExpand | |||||
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Ligands 3 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
NAG Query on NAG | D [auth A], E [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N | |||
FP1 Query on FP1 | B [auth A] | N-hydroxy-1-(1-methylpyridin-2(1H)-ylidene)methanamine C7 H10 N2 O YDWKOUCMHAMECR-SREVYHEPSA-N | |||
SO4 Query on SO4 | C [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |
Length ( ? ) | Angle ( ? ) |
---|---|
a = 113.95 | ¦Á = 90 |
b = 113.95 | ¦Â = 90 |
c = 138.05 | ¦Ă = 120 |
Software Name | Purpose |
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REFMAC | refinement |
DENZO | data reduction |
SCALEPACK | data scaling |
PROTIN | phasing |