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 Protein Homology/analogY Recognition Engine V 2.0


New fold library entries added 2020 Apr 25

Fold library idPDB HeaderMoleculeTitle
c6tmxE_ 5.80 chaperone Chain: E: putative groel-like chaperonine protein;
c6upnF_ 10.00 cytosolic protein Chain: F: endophilin-b1;
c6nyeB_ 1.90 de novo protein Chain: B: design construct xax;
c6whlB_ 2.30 hydrolase Chain: B: beta-lactamase;
c6wajA_ 1.90 protein binding Chain: A: nle1;
c6tvpA_ 1.90 sugar binding protein Chain: A: alpha-maltose-1-phosphate synthase;
c6lceA_ 1.78 sugar binding protein Chain: A: abc transporter substrate binding component;
c6tv9E_ 1.89 unknown function Chain: E: protein nirf,protein nirf;
c6tg9A_ 3.24 oxidoreductase Chain: A: formate dehydrogenase subunit alpha;
c6t0bm_ 2.80 oxidoreductase Chain: M: cytochrome b-c1 complex subunit 2, mitochondrial;
c6tp9G_ 2.19 electron transport Chain: G: cytochrome c55x;
c6tgaD_ 3.26 oxidoreductase Chain: D: nad-dependent formate dehydrogenase subunit delta;
c6r2qB_ 2.70 electron transport Chain: B: uncharacterized protein;
c6lvuA_ 2.29 biosynthetic protein Chain: A: acyl carrier protein;
c6tj2B_ 1.32 hydrolase Chain: B: alpha/beta hydrolase;
c6vpxP_ 5.00 viral protein/immune system Chain: P: antibody pgt151 fab heavy chain;
c6whpA_ 2.25 transferase Chain: A: choline kinase;
c6r99A_ 2.70 unknown function Chain: A: ceroid-lipofuscinosis neuronal protein 5;
c6xteA_ 2.27 translocase Chain: A: importin-5;
c6sc4B_ 2.60 metal binding protein Chain: B: uncharacterized protein;
c6xxvF_ 2.20 immune system Chain: F: s2_1.2;
c6xubE_ 1.78 oxidoreductase Chain: E: chlorite dismutase;
c6tg9F_ 3.24 oxidoreductase Chain: F: formate dehydrogenase subunit beta;
c6qycC_ 2.29 electron transport Chain: C: decaheme c-type cytochrome, omca/mtrc family;
c6u6uR_ 2.31 cytokine Chain: R: interleukin-1 receptor-like 2;
c6whjC_ 2.65 transferase Chain: C: ribokinase;
c6pajA_ 2.00 membrane protein Chain: A: sensor protein srrb;
c6tg9D_ 3.24 oxidoreductase Chain: D: nad-dependent formate dehydrogenase subunit delta;
c6lxhB_ 2.07 surfactant protein Chain: B: ser-asp rich fibrinogen-binding, bone sialoprotein-binding
c6jr3A_ 14.50 hormone Chain: A: insulin a chain;
c7bvaB_ 2.30 ligase Chain: B: udp-n-acetylmuramate--l-alanine ligase;
c6k95C_ 2.29 transferase Chain: C: glutathione-specific gamma-glutamylcyclotransferase 2;
c6wgyB_ 2.30 transferase Chain: B: putative citrate synthase 2;
c6jr3K_ 14.50 hormone Chain: K: insulin a chain;
c6wipA_ 1.40 hydrolase Chain: A: beta-lactamase;
c6wj8C_ 2.59 transferase Chain: C: 4-aminobutyrate aminotransferase puue;
c6oz1A_ 1.97 oxidoreductase Chain: A: oxidoreductase;
c6tgaG_ 3.26 oxidoreductase Chain: G: formate dehydrogenase subunit gamma;
c6t0br_ 2.80 oxidoreductase Chain: R: cytochrome b-c1 complex subunit 7;
c6tkuA_ 1.80 hydrolase Chain: A: depolymerase kp32gp38;
c6sbxC_ 2.33 dna binding protein Chain: C: cdba;
c6winA_ 2.05 antimicrobial protein Chain: A: type 6 secretion amidase effector 2;
c6m4jA_ 1.80 oxidoreductase Chain: A: sspa complex protein;
c6uncC_ 2.50 hydrolase Chain: C: metallophos domain-containing protein;
c6jp9C_ 2.10 ligase Chain: C: gmp synthase [glutamine-hydrolyzing] subunit b;
c6wi5A_ 1.83 de novo protein Chain: A: de novo designed protein foldit4;
c6r2qA_ 2.70 electron transport Chain: A: cystathionine beta-synthase;
c6w2oA_ 1.55 lyase Chain: A: uroporphyrinogen decarboxylase;
c6jr3G_ 14.50 hormone Chain: G: insulin a chain;
c6sh6B_ 1.85 hydrolase Chain: B: nf-kappa-b-repressing factor;
c6theA_ 2.87 oxidoreductase Chain: A: copper-containing nitrite reductase;
c6ln3A_ 2.00 transferase Chain: A: adenylate kinase;
c6wjmA_ 1.00 hydrolase Chain: A: beta-lactamase;
c6sh7B_ 2.21 hydrolase Chain: B: nf-kappa-b-repressing factor;
c6jtgA_ 2.40 hydrolase Chain: A: dynamin-like 120 kda protein, mitochondrial,opa1 protein;
c6jr3E_ 14.50 hormone Chain: E: insulin a chain;
c6s7vA_ 3.30 transport protein Chain: A: mfs transporter;
c6jr3C_ 14.50 hormone Chain: C: insulin a chain;
c6jr3I_ 14.50 hormone Chain: I: insulin a chain;

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Please cite: The Phyre2 web portal for protein modeling, prediction and analysis
Kelley LA et al. Nature Protocols 10, 845-858 (2015) [paper] [Citation link]
© Structural Bioinformatics Group, Imperial College, London
Lawrence Kelley, Michael Sternberg 
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