Proteinase

spinqualitylabelsall models E. coli proteinase K (grey) complex with lactoferrin peptide (green) and Ca+2 (green) and nitrate ions (PDB code 2duj) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Proteinase (PRO) are enzymes which hydrolyze peptide bonds. They are classified by the amino acid site of their cleavage or by the pH at which they are active. PRO B is a serine protease. For more details see Streptomyces griseus proteinase B. PRO A is a carboxylproteinase. PRO K is a serine protease which cleaves proteins preferentially after hydrophobic residues. Calcium ions contribute to the stability of the enzyme. PRO K is active over a wide pH range and is used in molecular biology to inactivate nucleases from preparations of DNA or RNA. PRO K is used in the partial proteolysis of lactoferrin into its N- and C-lobe. The two lobes of lactoferrin have different antimicrobial and antifungal properties. PRO K can digest hair (keratin).

3D structures of proteinase

Updated on 21-May-2015

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• Proteinase A
  • Streptomyces griseus proteinase B – SgPRO – Streptomyces griseus
    
  • 2jxr, 1fmu, 1fmx – yPRO - yeast
    
  • 1sgc - SgPRO + chymostatin A
    
  • 3sga, 4sga, 5sga - SgPRO + polypeptide inhibitor
    
  • 1dp5, 1dpj, 1g0v - yPRO + polypeptide inhibitor IA3
    
  • 1fq5 - yPRO + inhibitor
    
  • 4fvd – hevPRO 2A + peptide – human enterovirus
    
  • 4fvb – hevPRO 2A (mutant)
    
• Proteinase B
  • 3sgb – SgPRO + turkey ovomucoid inhibitor
    
  • 1sgp, 1sgq, 1sgr, 1cso, 1ct0, 1ct2, 1ct4, 1ds2, 2sgp, 2nu3, 2nu4 – SgPRO + turkey ovomucoid inhibitor (mutant)
    
  • 4sgb - SgPRO + potato inhibitor
• Proteinase K
  • 2prk, 1cnm, 1egq, 2id8, 2g4v, 2v8b, 3gt3, 3gt4, 3d9q, 3ddz, 3de0 , 3de1, 3de2, 3de3, 3de4, 3de5, 3de6, 3de7, 3dvq, 3dvr, 3dvs, 3dw1, 3dw3, 3dwe, 3i2y, 3i30, 3i37, 3i34, 3l1k, 3aj8, 3aj9, 3q40, 3q5g, 3qmp, 4b5l, 4fon – EaPRO + Ca – Engyodontium album
    
  • 1ic6 – EaPRO (mutant) + Ca
    
  • 1ptk, 1ht3 – EaPRO + Ca + Hg
    
  • 2pkc – EaPRO + Na
    
  • 4dj5, 4woc, 4wob – EaPRO
    
• Proteinase K complex with peptide
  • 3prk, 1p7v, 1p7w – EaPRO + Ca + peptide inhibitor
    
  • 1bjr, 2dqk, 2duj – EaPRO + Ca + lactoferrin peptide
    
  • 2hd4 – EaPRO + Ca + lactoferrin peptide inhibitor
    
  • 2dp4, 3ptl – EaPRO + lactoferrin peptide
    
  • 1pek, 1pfg, 4zar – EaPRO + peptide inhibitor
    
  • 1pj8 – EaPRO + Hg + substrate analog peptide
    
  • 2hpz, 2pq2 – EaPRO + Ca + peptide
    
  • 3osz – EaPRO + Ca + antimicrobial peptide
    
  • 2b6n – PRO + tripeptide - Serratia
    
• Proteinase K complex with small molecule
  • 2pwb – EaPRO + Ca + coumarin
    
  • 2pyz – EaPRO + Ca + auramine
    
  • 2pwa – EaPRO + Ca + alanine boronic acid
    
  • 1oyo – EaPRO + Ca + melanin monomer
    
  • 3dyb – EaPRO + Ca + digalacturonic acid
    
• Proteinase 3C
  • 1qa7 – PRO – Hepatitis virus
    
  • 2vb0, 3zyd - PRO – Coxsakievirus
    
  • 3zye – csvPRO (mutant)
    
  • 3zzd, 3zzc, 3zza, 3zzb, 3zz8, 3zz9, 3zz7, 3zz5, 3zz3, 3zz4 – csvPRO (mutant) + inhibitor
    
  • 4ghq – hevPRO
    
  • 4ght – hevPRO + common cold drug
    
• H2-Proteinase
  • 1wni – PRO – Trimeresurus flavoviridis
• Aspartic Proteinase
  • 2asi – PRO – Rhizomucor miehei
    
  • 1zap – CaPRO – Candida albicans
    
  • 1izd - AoPRO – Aspergillus oryzae
    
  • 1eag – CaPRO + inhibitor
    
  • 1fq4 - yPRO + inhibitor
    
  • 1j71 - PRO + polypeptide inhibitor – Candida tropicalis
    
  • 1ize - AoPRO + polypeptide-statin inhibitor
    
  • 1wkr - PRO + polypeptide-statin inhibitor – Irpex lacteus
• Cysteine Proteinase
  • 2hrv – PRO 2A – human rhinovirus
• Serine Proteinase
  • 1s2n, 1sh7 – PRO – Vibrio
    
  • 3s9a, 3s9b – RvPRO – Siamese Russell’s viper
    
  • 3s9c, 3sbk – RvPRO + human factor V polypeptide
    
  • 1ga1, 1ga4, 1ga6, 1nlu – PsPRO + iodotyrostatin fragment – Pseudomonas
    
  • 1kdv, 1kdy, 1kdz, 1ke1, 1ke2 - PsPRO + polypeptide inhibitor

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Joel L. Sussman, Karsten Theis