1i78 Summary



The structure was published by Vandeputte-Rutten, L., Kramer, R.A., Kroon, J., Dekker, N., Egmond, M.R., and Gros, P., in 2001 in a paper entitled "Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2001.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of PROTEASE VII.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PROTEASE VII P09169 (21-317) (OMPT_ECOLI)search Escherichia coli K-12search 100% 297 100%
B PROTEASE VII P09169 (21-317) (OMPT_ECOLI)search Escherichia coli K-12search 100% 297 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P09169 (21 - 317) PROTEASE VII Escherichia coli K-12

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P09169) Outer membrane protease OMPTsearch OMPT-likesearch PF01278: Omptin familysearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, B (P09169) endopeptidase activitysearch serine-type endopeptidase activitysearch peptidase activitysearch hydrolase activitysearch aspartic-type endopeptidase activitysearch cell outer membranesearch intrinsic component of cell outer membranesearch integral component of membranesearch membranesearch proteolysissearch

Chain InterPro annotation
A, B Peptidase A26, omptinsearch Peptidase A26, omptin, conserved sitesearch Outer membrane adhesin/peptidase omptinsearch Peptidase A26search