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 Protein Homology/analogY Recognition Engine V 2.0


New fold library entries added 2020 Apr 18

Fold library idPDB HeaderMoleculeTitle
c6u5hC_ 4.00 unknown function Chain: C: probable bacteriophage protein pyocin r2;
c6okdC_ 1.85 transport protein/signaling protein Chain: C: transferrin receptor binding cystine-dense peptide;
c6wc9A_ 2.64 transport protein Chain: A: endosomal/lysosomal potassium channel tmem175;
c6u5jD_ 3.50 antimicrobial protein Chain: D: collar pa0615;
c6jw6B_ 2.80 oxidoreductase Chain: B: dehydrogenase;
c6l07L_ 3.60 lyase Chain: L: phosphatidylserine decarboxylase alpha chain;
c6vjbA_ 2.24 immune system Chain: A: putative cell envelope proteinase;
c6vtwA_ 2.60 immune system Chain: A: s4_2.45;
c6lt0D_ 3.20 protein binding Chain: D: wd repeat-containing protein 41;
c6l07I_ 3.60 lyase Chain: I: phosphatidylserine decarboxylase alpha chain;
c6lypB_ 3.30 membrane protein Chain: B: mechanosensitive ion channel protein 1, mitochondrial;
c6kmfB_ 3.60 cell adhesion Chain: B: major fimbrium subunit fima type-1;
c6wfmA_ 1.95 transferase Chain: A: udp-n-acetylglucosamine 1-carboxyvinyltransferase;
c6w3dA_ 1.38 biosynthetic protein Chain: A: rd1ntf2_05;
c6lt0B_ 3.20 protein binding Chain: B: guanine nucleotide exchange protein smcr8;
c6lr0U_ 3.50 membrane protein Chain: U: bile salt export pump;
c6l54A_ 3.43 transferase/transcription Chain: A: serine/threonine-protein kinase smg1;
c7bqwB_ 2.50 lyase Chain: B: l-methionine gamma-lyase;
c6vvrA_ 1.80 isomerase Chain: A: tautomerase;
c6rcxB_ 2.00 transferase/transport protein Chain: B: phthiocerol synthesis polyketide synthase type i ppsc;
c6ok0A_ 2.17 hydrolase Chain: A: sel1 repeat protein;
c6r5nA_ 2.00 hydrolase Chain: A: periplasmic beta-glucosidase;
c6l07B_ 3.60 lyase Chain: B: phosphatidylserine decarboxylase beta chain;
c6o8jX_ UNK antimicrobial protein Chain: X: circular bacteriocin, circularin a/uberolysin family;
c6vkmA_ 3.50 viral protein Chain: A: virion spike glycoprotein;
c6w2wA_ 2.21 biosynthetic protein Chain: A: junction 24 dhr14-dhr18;
c6k1tA_ 1.58 hydrolase Chain: A: alpha/beta hydrolase fold family protein;
c6knyA_ 2.10 unknown function Chain: A: protein amuc_1100;
c6w2rB_ 2.34 biosynthetic protein Chain: B: junction 19 dhr54-dhr79;
c6w2qA_ 1.80 biosynthetic protein Chain: A: junction 34;
c6v88A_ UNK protein binding Chain: A: scf ubiquitin ligase complex protein skp1a;
c6xxqA_ 3.00 transferase Chain: A: streptomycin 3''-adenylyltransferase;
c6torB_ 2.05 lyase Chain: B: ethanolamine-phosphate phospho-lyase;
c6vvwE_ 2.10 isomerase Chain: E: tautomerase;
c6rl1A_ 1.70 sugar binding protein Chain: A: arabino-oligosaccharids-binding protein;
c6l3qA_ 2.70 nuclear protein Chain: A: wd_repeats_region domain-containing protein;
c6o8tX_ UNK antimicrobial protein Chain: X: circular bacteriocin, circularin a/uberolysin family;
c6txtA_ UNK structural protein Chain: A: competence pilin-like protein comgc;
c6lxdC_ 3.90 hydrolase/rna binding protein/rna Chain: C: microprocessor complex subunit dgcr8;
c6skiA_ 2.60 hydrolase Chain: A: putative type vi secretion protein;
c6k41R_ 2.90 membrane protein Chain: R: alpha-2a adrenergic receptor,endolysin,alpha-2b adrenergic
c6ok3A_ 2.35 hydrolase Chain: A: sel1 repeat protein;
c6umlE_ 3.58 ligase Chain: E: sal-like protein 4;
c6w2vB_ 2.40 biosynthetic protein Chain: B: junction 23 dhr14-dhr18;
c6w7xA_ 1.90 transferase Chain: A: acetylornithine aminotransferase;
c6lt0C_ 3.20 protein binding Chain: C: guanine nucleotide exchange c9orf72;
c6w3gB_ 1.62 biosynthetic protein Chain: B: rd1ntf2_04;
c6skiF_ 2.60 hydrolase Chain: F: putative type vi secretion protein;
c6umlC_ 3.58 ligase Chain: C: protein cereblon;
c6xwiA_ UNK de novo protein Chain: A: s0_2.126;
c6lxeA_ 4.20 hydrolase/rna binding protein Chain: A: ribonuclease 3;
c6xwsC_ 4.36 cell cycle Chain: C: chromosome alignment defect 1,chromosome alignment defect
c6lxeC_ 4.20 hydrolase/rna binding protein Chain: C: microprocessor complex subunit dgcr8;

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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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