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Structural Information for 1muc

The following displays the crystal structure (as found in 1muc, 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 4 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 A.
Site 4 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).

Lys 167 A

Residues Contacting Lys167A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
17.87
(0.5668)
62.5 1 3

Lys 169 A

Residues Contacting Lys169A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
20.4988
(0.8641)
71.3 1 1

Glu 327 A

Residues Contacting Glu327A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
44.6477
(0.6923)
40.6 7 1

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