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Structural Information for 1ti6

The following displays the crystal structure (as found in 1ti6, 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 29 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 C.
Site 3 covers chain E.
Site 4 covers chain G.
Site 5 covers chain I.
Site 6 covers chain K.
Site 7 covers chain A.
Site 8 covers chain C.
Site 9 covers chain E.
Site 10 covers chain G.
Site 11 covers chain I.
Site 12 covers chain K.
Site 13 covers chain A.
Site 14 covers chain C.
Site 15 covers chain E.
Site 16 covers chain G.
Site 17 covers chain I.
Site 18 covers chain K.
Site 19 covers chain A.
Site 20 covers chain C.
Site 21 covers chain E.
Site 22 covers chain G.
Site 23 covers chain I.
Site 24 covers chain A.
Site 25 covers chain C.
Site 26 covers chain E.
Site 27 covers chain G.
Site 28 covers chain I.
Site 29 covers chain K.


The Catalytic Domains:

  • There are 3 catalytic residues within an unassigned CATH domain: His144A, Asp174A, Tyr404A

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 144 A

Residues Contacting His144A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
41.844
(0.0052)
0 2 4

Asp 174 A

Residues Contacting Asp174A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
44.5712
(0.934)
85.1 5 1

Tyr 404 A

Residues Contacting Tyr404A

B Factor
(normalised)
Relative Solvent Accessibility Number of H-Bond Donors Number of H-Bond Acceptors
10.895
(0.1222)
4.2 5 4

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