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Structural Information for 1ptd

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

His 32 A

Residues Contacting His32A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
4.183
(0.0135)
13.5 2 2

Asp 33 A

Residues Contacting Asp33A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
27.81
(0.3452)
0.4 2 1

Arg 69 A

Residues Contacting Arg69A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
5.7336
(0.0992)
8 1 2

His 82 A

Residues Contacting His82A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
24.482
(0.462)
1.5 1 1

Asp 274 A

Residues Contacting Asp274A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
8.23
(0.1351)
2.1 3 1

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