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Structural Information for 1afr

The following displays the crystal structure (as found in 1afr, 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 6 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.
Site 3 covers chain C.
Site 4 covers chain D.
Site 5 covers chain E.
Site 6 covers chain F.


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).

Trp 62 A

Residues Contacting Trp62A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
32.475
(0.3888)
45.1 1 1

His 146 A

Residues Contacting His146A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
22.786
(0.5078)
13.9 1 2

Thr 199 A

Residues Contacting Thr199A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
24.4157
(0.0824)
3.7 1 2

Asp 228 A

Residues Contacting Asp228A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
23.5125
(0.6171)
48.9 4 2

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