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Structural Information for 1bjp

The following displays the crystal structure (as found in 1bjp, 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 10 catalytic sites (as determined by the Catalytic Site Atlas), only one of which is shown highlighed by CATH domain.
Site 1 covers chains A and B.
Site 2 covers chain A.
Site 3 covers chain C.
Site 4 covers chain D.
Site 5 covers chain E.
Site 6 covers chains A and B.
Site 7 covers chain B.
Site 8 covers chain C.
Site 9 covers chain D.
Site 10 covers chain E.


The Catalytic Domains:

  • There are 3 catalytic residues within an unassigned CATH domain: Pro1A, Phe50A, Arg39B

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).

Pro 1 A

Residues Contacting Pro1A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
12.1214
(0.1513)
139.4 2 0

Phe 50 A

Residues Contacting Phe50A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
10.2354
(0.0921)
9.1 1 0

Arg 39 B

Residues Contacting Arg39B

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
15.4554
(0.2656)
3.5 1 2

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