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Structural Information for 1b6t

The following displays the crystal structure (as found in 1b6t, 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).

Arg 91 A

Residues Contacting Arg91A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
25.2618
(0.4166)
0.8 1 3

Lys 42 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
8.0261
(0.7088)
82 0 0

His 18 A

Residues Contacting His18A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
17.739
(0.6161)
22.5 5 1

Ser 129 A

Residues Contacting Ser129A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
33.7766
(0.6379)
1.2 2 1

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