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Structural Information for 1f61

The following displays the crystal structure (as found in 1f61, 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 2 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.


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).

Ser 315 A

Residues Contacting Ser315A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
33.015
(0.8725)
42.9 3 1

Ser 317 A

Residues Contacting Ser317A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
98.0366
(0.9279)
50.4 1 1

His 193 A

This residue does not appear to have any contacts to other species in the PDB file.

.
B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
39.971
(0.826)
47.7 0 0

Cys 191 A

Residues Contacting Cys191A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
55.4416
(0.9796)
4.9 1 0

Arg 228 A

Residues Contacting Arg228A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
47.8572
(0.0633)
37.7 1 5

His 180 A

Residues Contacting His180A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
43.581
(0.7301)
20.6 3 3

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