Lipase 3D Structures

3D Structures of Lipase

Updated on 22-October-2019

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• Eukaryote lipase:
  • 1hpl – hLip – horse
    
  • 1hlg – hLip – human - gastric
    
  • 1jmy – hBSSL
    
  • 1akn – cBSSL – cattle
    
  • 2bce - cBSSL (mutant)
    
  • 1f6w - cBSSL – catalytic domain
    
  • 3o0d – Lip – Yarrowia lipolytica
    
  • 4jei – YlLip (mutant)
    
  • 1gpl – Lip – Guinea pig
    
  • 3zpx – Lip – Ustilago maydis
    
  • 6a0w – Lip catalytic domain – bread mold
    
  • 4zrd, 4zre – Lip1 (mutant) – dandruff fungus
    
• Prokaryote lipase:
  • 1llf – Lip – Candida cylindracea
    
  • 3g7n – Lip - Penicillium expansum
    
  • 1tia - Lip – Penicillium camemberti
    
  • 2hih – Lip – Staphylococcus hyicus
    
  • 2fx5 – Lip – Pseudomonas mendocina
    
  • 1yzf – Lip – Enterococcus faecalis
    
  • 1dt3, 1dt5, 1dte, 1du4, 1ein, 1tib, 4dyh, 4ea6, 4flf, 4gbg, 4gwl, 4zgb, 6hw1 - TlLip - Thermomyces lanuginose
    
  • 5ap9 – TlLip (mutant)
    
  • 1jfr – Lip – Streptomyces exfoliates
    
  • 5mal – Lip – Streptomyces rimosus
    
  • 2lip – BcLip – open state
    
  • 1cvl – Lip – Chromobacterium viscosum
    
  • 1tic - Lip – Rhizopus oryzae
    
  • 3tgl, 4tgl, 1tgl, 6qpp – RmLip – Rhyzomucor miehei
    
  • 6qpr – RmLip (mutant)
    
  • 2zvd – PsLip - Pseudomonas sp. – open state
    
  • 2z8x - PsLip – extracellular
    
  • 5xpx – PsLip residues 1-388
    
  • 2zj6, 2zj7 – PsLip (mutant)
    
  • 2z8z – PsLip(mutant) – closed state
    
  • 3lip, 3a6z - Lip - Pseudomonas cepacia – open state
    
  • 1qge, 1tah – Lip – Pseudomonas glumae
    
  • 2w22, 6a12 – GtLip – Geobacillus thermocatenulatus
    
  • 5ce5 – GtLip (mutant)
    
  • 1ji3, 1ku0, 4fmp, 4x6u – BstLip – Bacillus stearothermophilus
    
  • 4x71, 4x7b, 4x85, 6s3g, 6s3j, 6s3v, 6fz1, 6fz7, 6fz8, 6fz9, 6fza, 6fzc, 6fzd – BstLip (mutant)
    
  • 1ah7 - Lip – Bacillus cereus
    
  • 2ory – Lip – Photobacterium lypoliticum
    
  • 2z5g, 2dsn – GzLip T1 – Geobacillus zalihae
    
  • 3umj – GzLip (mutant)
    
  • 3p94 – Lip – Parabacteroides distasonis
    
  • 3ngm – Lip – Gibberella zeae
    
  • 3auk - Lip – Geobacillus
    
  • 3uue, 3uuf – Lip – Malassezia globosa
    
  • 4hs9 – Lip – Proteus mirabilis
    
  • 4opm – Lip – Acinetobacter baumannii
    
  • 5ah0 – Lip – Pelosinus fermentans
    
  • 5ah1 – Lip – Clostridium botulinum
    
  • 5ch8 – Lip (mutant) – Penicillium cyclopium
    
• Bacterial lipase A
  • 3guu – CaLipA – Candida Antarctica
    
  • 2veo – CaLipA – closed state
    
  • 2qua, 2qub – SmLipA – Serratia marcescens
    
  • 2qxt, 2qxu, 1isp, 1i6w, 5ct4, 5ct5, 5ct6, 5cri - BsLipA – Bacillus subtilis
    
  • 3d2a, 3d2b, 3d2c, 1t2n, 1t4m, 5ct8, 5ct9, 5cta, 5cur, 3qzu, 3qmm - BsLipA (mutant)
    
  • 1r4z – BsLipA+Rc-IPG-phosphonate
    
  • 1r50 – BsLipA +Sc-IPG-phosphonate
    
• Bacterial lipase B
  • 4zv7, 3w9b, 5a6v, 5a71, 4k6g, 1tca, 1tcb, 1tcc, 1lbs, 1lbt – CaLipB
    
  • 3icv, 4k5q, 5k6h, 5k6k – CaLipB (mutant)
    
  • 5gv5 - CaLipB + phosphonate
    
  • 3icw – CaLipB (mutant) + phosphonate
    
  • 5x7k – SmLipB NBD
    
  • 6isp, 6isq, 6isr – LipB (mutant) – Pseudozyma antarctica
    
  • 6idy - AfLipB - Aspergillus fumigatus
    
• Bacterial lipase C
  • 5nen – SmLipC residues 1-443
    
• Lipase/colipase complexes. The colipase is a co-enzyme whose binding to lipase optimizes the enzymatic activity
  • 1n8s – hLip+colipase II
    
  • 1eth, 1lpa - pLip+colipase II - pig
    
• Hormone-sensitive-lipases (LIPE) hydrolyze the first fatty acid of the triacylglycerol substrate
  • 3k6k – EstE7(LIPE) – metagenome library
    
  • 3fak, 3dnm – EstE5(LIPE) – metagenome library
    
  • 1evq – AaEst2(LIPE) – Alicyclobacillus acidocaldarius
    
  • 1u4n – AaEst2(LIPE) (mutant)
    
• Putative lipases; Proteins with unknown function but structural similarity to lipase obtained in structural genomics projects.
  • 2rau - Lip – Sulfolobus solfataricus
    
  • 3bxp, 3d3n - Lip – Lactobacillus plantarum
    
  • 3e0x - Lip – Clostridium acetobutylicum
    
  • 1z8h – Lip – Nostoc sp. PCC 712
    
  • 1vj3 - Lip – Nostoc sp.
    
  • 3bzw – Lip - Bacteroides thetaiotaomicron
    
  • 2pbl – Lip - Silicibacter
• Lipase + inhibitors
  • 3l1h – EstE5(LIPE)+FeCl3 – noninvasive inhibitor
    
  • 3l1i, 3l1j - EstE5(LIPE)+CuSO4 – noninvasive inhibitor
    
  • 3lij - EstE5(LIPE)+ZnSO4– noninvasive inhibitor
    
  • 3h18, 3h17 - EstE5 (LIPE)+PMSF
    
  • 3h19, 3h1b, 3h1a – EstE5 (LIPE)+methyl alcohol
    
  • 3h1a – EstE5 SLIPE)+ethyl alcohol
    
  • 3h19 – EstE5 SLIPE)+isopropyl alcohol
    
  • 3g9t, 3g9u - EstE5 (HSLIPE)+p-nitrophenyl butyrate
    
  • 3g9z - EstE5 (LIPE) +p-nitrophenyl caprylate
    
  • 2nw6 – BcLip+ S inhibitor
    
  • 4lip, 5lip, 1r4z, 1r50 – BcLip+ Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate
    
  • 1k8q - Lip+phosphonate – dog
    
  • 1ex9 – Lip+Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate – Pseudomonas aeruginosa
    
  • 5tgl – RmLip+N-hexyl-phosphonate
    
  • 1lpb – pLip + colipase+C11 alkyl phosphonate
    
  • 3a70 – PsLip+diethyl phosphate
    
  • 4glb – TlLip + nitrobenzaldehyde
    
  • 4kjx - TlLip + nitrobenzaldehyde + lauric acid
    
  • 4n8s - TlLip + nitrobenzaldehyde + ethylacetoacetate
    
  • 4s0x – TlLip + lauric acid
    
• Lipase conjugated with analogs to its reaction intermediates
  • 1qz3 – EaEst2(mutant) (LIPE)+hexadecanesulfonate
    
• Bile-salt activated lipase
  • 6h0t – hBAL (mutant)
    
  • 6h0v, 6h18, 6h19, 6h1a – hBAL (mutant) + nerve agent
    
  • 1aql – bBAL+taurocholate - bovine
    
• Monoacylglycerol lipase
  • 3hju, 3jw8 - hMAGL
    
  • 3jwe, 3pe6, 4uuq, 6ax1, 6bq0 – hMAGL + inhibitor
    
  • 4uuq - hMAGLip + SAR
    
  • 5zun – hMAGL (mutant) + inhibitor
    
  • 3rm3, 4lhe, 5xks - BaMAGL – Bacillus
    
  • 3rli – BaMAGL + PMSF
    
  • 4ke7, 4ke8, 4ke9 – BaMAGL + ligand
    
  • 4ke6, 4kea – BaMAGL (mutant) + ligand
    
  • 4zwn – yMAGL – yeast
    
  • 4zxf – yMAGLip + substrate analog
    
  • 6eic – MAGLip – Mycobacterium tuberculosis
    
  • 5xk2 – MAGLip – Aespergillus oryzae
    
• Lipase with substrate bound at active site
  • 2zyh – AfLip (mutant)+fatty acid – Archaeoglobus fulgidus
    
  • 2zyi, 2zyr, 2zys - AfLip+fatty acid+ ion
    
  • 1gt6, 4ghw, 4gi1 – TlLip+ fatty acid - lipid ligand
    
• Lipase conjugated to transition-state analogs showing the binding mode of the enzyme catalysis
  • 1ys1 – BhLip+hexylphosphonic acid (R) 2-methyl-3-phenylpropyl ester
    
  • 1ys2 – BhLip+hexylphosphonic acid (S) 2-methyl-3-phenylpropyl ester
    
  • 1hqd – Lip+1-phenoxy-2-acrtoxy butane – Pseudomonas cepacia
    
• Lipase+lipase chaperone
  • 2es4 – Lip+lipase chaperone C-terminal - Burkholderia glumae
• Lipase 2 or esterase/lipase
  • 3v9a,3g9t, 3g9u, 3g9z, 3h19, 3h1a, 3h1b, 3l1h, 3l1i, 3l1j, 3fak, 3h17, 3h18, 3dnm, 3k6k - E/L - uncultured bacteria
    
  • 3w9b - CaE/L
    
  • 4v2i - E/L - Thalassospira
    
  • 4n5h - LrE/L (mutant) - Lactobacillus rhamnosus
    
  • 4n5i - LrE/L + inhibitor
    
  • 4ouk - LrE/L (mutant) + inhibitor
    
  • 4bzz, 4bzw - LpE/L
    
  • 6gup - AfE/L
    
  • 1lgy – Lip2 – Rhizopus niveus
    
  • 1gz7 - CrLip2
    
  • 4jei – Lip2 – Yarrowia lipolytica
    
  • 1thg – Lip2 – Geotrichum candidum
    

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Michal Harel, Joel L. Sussman