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Structural Information for 2eua

The following displays the crystal structure (as found in 2eua, 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:

  • There are 5 catalytic residues within an unassigned CATH domain: Lys420A, Glu416A, Glu284A, Lys190A, Glu240A

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 420 A

Residues Contacting Lys420A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
21.3844
(0.3221)
7.1 1 1

Glu 416 A

Residues Contacting Glu416A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
11.5377
(0.6114)
74.1 1 1

Glu 284 A

Residues Contacting Glu284A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
47.9
(0.8831)
70.3 1 1

Lys 190 A

Residues Contacting Lys190A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
51.5433
(0.8769)
52.9 1 1

Glu 240 A

Residues Contacting Glu240A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
19.2244
(0.9201)
60.4 3 1

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