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Structural Information for 1hzz

The following displays the crystal structure (as found in 1hzz, 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 3 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 chain C.


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).

Arg 127 A

Residues Contacting Arg127A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
45.4327
(0.8915)
52.6 0 1

Asp 135 A

Residues Contacting Asp135A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
62.4175
(0.9728)
37.6 4 2

Tyr 235 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
15.2483
(0.0235)
0 0 0

Asp 132 C

Residues Contacting Asp132C

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
25.4387
(0.4652)
0.6 2 1

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