Mechanisms of Enzyme-Catalyzed Deprotonation of Acetyl-Coenzyme A
Schwartz, B., Vogel, K.W., Usher, K.C., Narasimhan, C., Miziorko, H.M., Remington, S.J., Drueckhammer, D.G.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 |
CITRATE SYNTHASE | 435 | Gallus gallus | Mutation(s): 0  EC: 4.1.3.7 (PDB Primary Data), 2.3.3.1 (UniProt) | ||
UniProt | |||||
Find proteins for P23007 (Gallus gallus) Explore P23007  Go to UniProtKB:  P23007 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P23007 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 2 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
NMX Query on NMX | C [auth A] | NITROMETHYLDETHIA COENZYME A C22 H37 N8 O18 P3 PUGKTLRHGHIDCJ-GORZOVPNSA-N | |||
MLT Query on MLT | B [auth A] | D-MALATE C4 H6 O5 BJEPYKJPYRNKOW-UWTATZPHSA-N |
Length ( ? ) | Angle ( ? ) |
---|---|
a = 104.127 | ¦Á = 90 |
b = 78.5 | ¦Â = 78.93 |
c = 58.42 | ¦Ă = 90 |
Software Name | Purpose |
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TNT | refinement |
SDMS | data reduction |
SDMS | data scaling |
TNT | phasing |