2dp4

Crystal structure of the complex formed between proteinase K and a human lactoferrin fragment at 2.9 A resolutionCrystal structure of the complex formed between proteinase K and a human lactoferrin fragment at 2.9 A resolution

Structural highlights 2dp4 is a 2 chain structure with sequence from Engyodontium album and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3prk, 1bjr Activity: Peptidase K, with EC number 3.4.21.64 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PRTK_TRIAL] Hydrolyzes keratin at aromatic and hydrophobic residues. [TRFL_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration. Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors. 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. Isoform DeltaLf: transcription factor with antiproliferative properties and inducing cell cycle arrest. Binds to DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Proteinase Proteinase 3D structures

spinqualitylabelsall models 2dp4, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image