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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j4u ConSurf]. | ||
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Revision as of 02:15, 8 February 2016
E.coli OmpC - camel Lactoferrin complexE.coli OmpC - camel Lactoferrin complex
Structural highlights
Function[OMPC_ECOLI] Forms pores that allow passive diffusion of small molecules across the outer membrane. [TRFL_CAMDR] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate (By similarity). The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity (By similarity). Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Camelus dromedarius
- Escherichia coli
- Acharya, R K
- Baalaji, S
- Krishnaswamy, S
- Singh, T P
- Antiacterial peptide
- Complex
- Glycoprotein
- Hydrolase
- Ion transport
- Iron
- Iron transport
- Lactoferrin
- Membrane protein
- Membrane protein-hydrolase complex
- Membrane protein/hydrolase
- Metal-binding
- Ompc
- Porin
- Protease
- Serine protease
- Transport