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Structural Information for 1yrc

The following displays the crystal structure (as found in 1yrc, 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 A.


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 186 A

Residues Contacting Arg186A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
17.0063
(0.427)
39.5 1 4

Asp 251 A

Residues Contacting Asp251A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
2.8075
(0.1801)
13.2 5 1

Thr 252 A

Residues Contacting Thr252A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
2.9357
(0.2092)
0 3 2

Cys 357 A

Residues Contacting Cys357A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
11.03
(0.0395)
33.1 3 1

Leu 358 A

Residues Contacting Leu358A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
17.5537
(0.1014)
2.5 2 0

Gly 359 A

Residues Contacting Gly359A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
24.825
(0.6058)
3 2 1

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