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Structural Information for 1e79

The following displays the crystal structure (as found in 1e79, 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 9 catalytic sites (as determined by the Catalytic Site Atlas), only one of which is shown highlighed by CATH domain.
Site 1 covers chain E.
Site 2 covers chain F.
Site 3 covers chain D.
Site 4 covers chains A and E.
Site 5 covers chains F and B.
Site 6 covers chains C and D.
Site 7 covers chain A.
Site 8 covers chain B.
Site 9 covers chain C.


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 162 D

Residues Contacting Lys162D

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
35.7666
(0.0377)
9.8 2 3

Glu 188 D

Residues Contacting Glu188D

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
19.4333
(0.6113)
31.4 5 0

Arg 189 D

Residues Contacting Arg189D

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
40.4463
(0.206)
2.9 2 3

Arg 373 C

Residues Contacting Arg373C

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
50.41
(0.7179)
55.5 0 4

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