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Structural Information for 1pym

The following displays the crystal structure (as found in 1pym, 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 159 A

Residues Contacting Arg159A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
6.2675
(0.6076)
34 1 4

Ser 46 A

Residues Contacting Ser46A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
9.3916
(0.0062)
0 2 3

Leu 48 A

Residues Contacting Leu48A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
11.7362
(0.0049)
0 2 1

Ser 123 A

Residues Contacting Ser123A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
28.0516
(0.8878)
48.4 4 4

Asn 122 A

Residues Contacting Asn122A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
8.245
(0.0242)
28.4 3 2

His 190 A

Residues Contacting His190A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
23.366
(0.7802)
76.3 2 2

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