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Structural Information for 1n20

The following displays the crystal structure (as found in 1n20, 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).

Trp 323 A

Residues Contacting Trp323A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
9.3764
(0.5344)
11.5 2 2

Phe 578 A

Residues Contacting Phe578A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
39.5918
(0.4205)
2.7 1 1

Ile 344 A

Residues Contacting Ile344A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
29.3977
(0.8666)
49.6 1 1

Val 452 A

Residues Contacting Val452A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
21.5485
(0.5695)
0.7 1 1

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