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Structural Information for 1req

The following displays the crystal structure (as found in 1req, 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 10 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 C.
Site 3 covers chain B.
Site 4 covers chain D.
Site 5 covers chain A.
Site 6 covers chain C.
Site 7 covers chain A.
Site 8 covers chain C.
Site 9 covers chain A.
Site 10 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).

Tyr 89 A

Residues Contacting Tyr89A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
18.5966
(0.4037)
0.3 2 3

His 244 A

Residues Contacting His244A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
18.754
(0.4007)
31.3 3 2

Lys 604 A

Residues Contacting Lys604A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
30.8422
(0.3941)
1.9 2 4

Asp 608 A

Residues Contacting Asp608A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
34.6525
(0.3532)
3.1 5 1

His 610 A

Residues Contacting His610A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
33.425
(0.3153)
51.1 2 1

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