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Structural Information for 1mum

The following displays the crystal structure (as found in 1mum, 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).

Asp 58 A

Residues Contacting Asp58A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
47.3925
(0.9094)
65.3 5 1

Cys 123 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
5.4483
(0.1596)
0.8 0 0

Arg 158 A

Residues Contacting Arg158A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
21.4718
(0.3287)
21.8 1 4

Glu 188 A

Residues Contacting Glu188A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
33.2977
(0.78)
46 5 1

Asn 210 A

Residues Contacting Asn210A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
37.2775
(0.5833)
92.6 1 2

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