PDB ID or protein name

1i78 » Outer membrane protease OmpT

1i78 » Outer membrane protease OmpT
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Topology in Bacterial Gram-negative outer membrane
Topologyout side
in side
1i78 » Outer membrane protease OmpT
Hydrophobic Thickness 26.5 ± 1.6 Å
Tilt Angle 5 ± 6°
ΔGtransfer -46.9 kcal/mol
Links to 1i78 PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology subunit A (N-terminus in)
Resolution 2.6 Å
Other PDB entries representing this structure none
Number of TM Secondary Structures 10
1 transmembrane subunit
A - Tilt: 3° - Segments: 1(11-20), 2(50-61), 3(64-72), 4(111-121), 5(126-136), 6(178-187), 7(192-201), 8(230-240), 9(245-254), 10(287-296)
Comments on 1i78 » Outer membrane protease OmpT
This aspartic peptidase is distinct from trypsin-like proteases becase it cleaves polypeptides between two basically-charged amino acids. The enzyme is sensitive to the serine protease inhibitor diisopropylfluoro-phosphate, to divalent cations such as Cu2+, Zn2+ and Fe2+, and its activity decreases at lower temperatures. OmpT is not a a serine protease with Ser(99) and His(212) as active site residues, but rather a aspartic endopeptidase whose activity is also strongly dependent on Asp(83) and Asp(85). Both acids may function in binding of the water molecule and/or oxyanion stabilisation.