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Structural Information for 1fwj

The following displays the crystal structure (as found in 1fwj, 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 C.
Site 2 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).

Kcx 217 C

Residues Contacting Kcx217C

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors

()
1 2

His 219 C

Residues Contacting His219C

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
9.136
(0.3537)
20.1 5 3

Asp 221 C

Residues Contacting Asp221C

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
10.3187
(0.4621)
1.1 3 1

His 320 C

Residues Contacting His320C

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
2.957
(0.0638)
3.1 1 3

Arg 336 C

Residues Contacting Arg336C

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
28.3727
(0.7898)
35.4 1 3

Asp 360 C

Residues Contacting Asp360C

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
6.9175
(0.1501)
3.3 4 1

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