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Structural Information for 1fva

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

Cys 72 A

Residues Contacting Cys72A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
30.0216
(0.4488)
15.2 1 1

Tyr 103 A

Residues Contacting Tyr103A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
38.555
(0.8034)
34 3 2

Glu 115 A

Residues Contacting Glu115A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
9.8911
(0.5848)
0.6 4 1

Tyr 155 A

Residues Contacting Tyr155A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
19.7408
(0.4239)
5.9 2 2

Cys 218 A

Residues Contacting Cys218A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
73.405
(0.9875)
31.3 1 0

Cys 227 A

Residues Contacting Cys227A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
3.1716
(0.0525)
0 0 1

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