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Structural Information for 1mns

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

Lys 164 A

Residues Contacting Lys164A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
23.71
(0.3661)
17.7 1 5

Lys 166 A

Residues Contacting Lys166A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
14.8142
(0.8488)
56.5 2 2

Asp 270 A

Residues Contacting Asp270A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
24.155
(0.2383)
0 5 1

His 297 A

Residues Contacting His297A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
2.224
(0.028)
7.8 1 3

Glu 317 A

Residues Contacting Glu317A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
32.0577
(0.7006)
61.6 5 2

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