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Structural Information for 2vss

The following displays the crystal structure (as found in 2vss, 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 12 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 A.
Site 3 covers chain B.
Site 4 covers chain C.
Site 5 covers chain D.
Site 6 covers chain F.
Site 7 covers chain A.
Site 8 covers chain B.
Site 9 covers chain C.
Site 10 covers chain D.
Site 11 covers chain E.
Site 12 covers chain F.


The Catalytic Domains:

  • There are 4 catalytic residues within an unassigned CATH domain: Met70A, Tyr75A, Gly120A, Tyr239B

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).

Met 70 A

Residues Contacting Met70A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
37.4237
(0.8726)
14.4 1 1

Tyr 75 A

This residue does not appear to have any contacts to other species in the PDB file.

.
B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
22.6058
(0.5659)
31.6 0 0

Gly 120 A

Residues Contacting Gly120A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
14.9125
(0.4791)
4.4 2 1

Tyr 239 B

Residues Contacting Tyr239B

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
33.8783
(0.7808)
9.6 2 1

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