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![[Figure 2]](di5014fig2mag.jpg)
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Figure 2
Nucleotide binding in the active site of closed WalK. (a, b, c) Electron-density maps of bound nucleotides and His391. The simulated-annealing OMIT map is contoured at 2σ. An alternative rotamer conformation of His391 in the open chain is shown as grey sticks. Long distances between ∊N and βP/γP are highlighted by blue dashed lines. (d) Detailed interaction of AMPPCP and ADP in the active pocket of the CA domain. Key interacting residues are shown as sticks. Hydrogen bonds formed to AMPPCP are highlighted by yellow dashed lines and hydrogen bonds formed to βP in ADP are highlighted by green dashed lines. The backbone amines are shown as balls. (e) Aligned AMPPCP and ADP in the active pocket of the CA domain. AMPPCP is coloured green. ADP is coloured grey. The hydrogen bonds from AMPPCP/ADP to His391 ∊N are highlighted and labelled with the bond distances. (f) Modelled ATP in the active pocket of the CA domain. ATP was modelled into its pocket by alignment of lpWalK with the bsWalK–ATP complex. ATP is coloured grey. ADP from the lpWalK–ADP complex is coloured green. The possible hydrogen bonds between ATP γP and His391 ∊N are highlighted and their bond distances are also labelled. |
![[Figure 2]](di5014fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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