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Structural Information for 1q6l

The following displays the crystal structure (as found in 1q6l, the primary PDB code for the entry) with each catalytic domain highlighted. The catalytic residues are also highlighed in teal and shown in wireframe depiction. Domains which are not classified as catalytic are shown in grey.

This enzyme has 6 catalytic sites (as determined by the Catalytic Site Atlas), only one of which is shown highlighed by CATH domain.
Site 1 covers chain A.
Site 2 covers chain B.
Site 3 covers chains A, and B.
Site 4 covers chain B.
Site 5 covers chains A, and B.
Site 6 covers chain A.


The Catalytic Domains:

The Catalytic Residues

The following shows the catalytic residues (the catalytic residue in focus is labelled in red) and the residues which are donating hydrogen bonds (labelled in blue) and accepting hydrogen bonds (labelled in green).

Asp 67 B

Residues Contacting Asp67B

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
8.8075
(0.1263)
66.5 6 0

Glu 112 A

Residues Contacting Glu112A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
40.2733
(0.924)
32.8 4 1

Lys 64 A

Residues Contacting Lys64A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
12.4611
(0.028)
11.9 0 5

His 136 A

Residues Contacting His136A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
9.114
(0.1955)
1.3 3 5

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