General Structure Information 1r03 FTMT crystal structure of a human mitochondrial ferritin 1.7Å AUTH B.LANGLOIS DESTAINTOT,P.SANTAMBROGIO,T.GRANIER,B.GALLOIS,AUTH 2 J.M.CHEVALLIER,G.PRECIGOUX,S.LEVI,P.AROSIOTITL CRYSTAL STRUCTURE AND BIOCHEMICAL PROPERTIES OF THE HUMANTITL 2 MITOCHONDRIAL FERRITIN AND ITS MUTANT SER144ALAREF J.MOL.BIOL. V. 340 277 2004REFN ISSN 0022-2836PMID 15201052DOI 10.1016/J.JMB.2004.04.036 Variant Set Distributions Ripley’s K Analysis Plots Variant Set Comparisons Pathogenic Proximity Analysis […]
General Structure Information 2om5 CNTN2 n-terminal fragment of human tax1 3.07Å AUTH M.MORTL,P.SONDEREGGER,K.DIEDERICHS,W.WELTETITL THE CRYSTAL STRUCTURE OF THE LIGAND-BINDING MODULE OF HUMANTITL 2 TAG-1 SUGGESTS A NEW MODE OF HOMOPHILIC INTERACTIONREF PROTEIN SCI. V. 16 2174 2007REFN ISSN 0961-8368PMID 17766378DOI 10.1110/PS.072802707 Variant Set Distributions Ripley’s K Analysis Plots Variant Set Comparisons Mapped Variants
General Structure Information 1nud TGM3 role of calcium ions in the activation and activity of the transglutaminase 3 enzyme (3 calciums, active form) 2.7Å AUTH B.AHVAZI,K.M.BOESHANS,W.IDLER,U.BAXA,P.M.STEINERTTITL ROLES OF CALCIUM IONS IN THE ACTIVATION ANDTITL 2 ACTIVITY OF THE TRANSGLUTAMINASE 3 ENZYMEREF J.BIOL.CHEM. V. 278 23834 2003REFN ISSN 0021-9258PMID 12679341DOI 10.1074/JBC.M301162200 Variant Set Distributions Ripley’s K […]
General Structure Information 1esr CCL8 crystal structure of human monocyte chemotactic protein-2 2.0Å AUTH J.BLASZCZYK,E.V.COILLIE,P.PROOST,J.V.DAMME,AUTH 2 G.OPDENAKKER,G.D.BUJACZ,J.M.WANG,X.JITITL COMPLETE CRYSTAL STRUCTURE OF MONOCYTE CHEMOTACTICTITL 2 PROTEIN-2, A CC CHEMOKINE THAT INTERACTS WITHTITL 3 MULTIPLE RECEPTORS.REF BIOCHEMISTRY V. 39 14075 2000REFN ISSN 0006-2960PMID 11087354DOI 10.1021/BI0009340 Variant Set Distributions Mapped Variants
General Structure Information 2om5 CNTN2 n-terminal fragment of human tax1 3.07Å AUTH M.MORTL,P.SONDEREGGER,K.DIEDERICHS,W.WELTETITL THE CRYSTAL STRUCTURE OF THE LIGAND-BINDING MODULE OF HUMANTITL 2 TAG-1 SUGGESTS A NEW MODE OF HOMOPHILIC INTERACTIONREF PROTEIN SCI. V. 16 2174 2007REFN ISSN 0961-8368PMID 17766378DOI 10.1110/PS.072802707 Variant Set Distributions Ripley’s K Analysis Plots Variant Set Comparisons Mapped Variants
General Structure Information 1nud TGM3 role of calcium ions in the activation and activity of the transglutaminase 3 enzyme (3 calciums, active form) 2.7Å AUTH B.AHVAZI,K.M.BOESHANS,W.IDLER,U.BAXA,P.M.STEINERTTITL ROLES OF CALCIUM IONS IN THE ACTIVATION ANDTITL 2 ACTIVITY OF THE TRANSGLUTAMINASE 3 ENZYMEREF J.BIOL.CHEM. V. 278 23834 2003REFN ISSN 0021-9258PMID 12679341DOI 10.1074/JBC.M301162200 Variant Set Distributions Ripley’s K […]
General Structure Information 1esr CCL8 crystal structure of human monocyte chemotactic protein-2 2.0Å AUTH J.BLASZCZYK,E.V.COILLIE,P.PROOST,J.V.DAMME,AUTH 2 G.OPDENAKKER,G.D.BUJACZ,J.M.WANG,X.JITITL COMPLETE CRYSTAL STRUCTURE OF MONOCYTE CHEMOTACTICTITL 2 PROTEIN-2, A CC CHEMOKINE THAT INTERACTS WITHTITL 3 MULTIPLE RECEPTORS.REF BIOCHEMISTRY V. 39 14075 2000REFN ISSN 0006-2960PMID 11087354DOI 10.1021/BI0009340 Variant Set Distributions Mapped Variants
General Structure Information 2fs7 CRABP2 crystal structure of apo-cellular retinoic acid binding protein type ii at 1.55 angstroms resolution 1.55Å AUTH S.VAEZESLAMI,E.MATHES,C.VASILEIOU,B.BORHAN,AUTH 2 J.H.GEIGERTITL THE STRUCTURE OF APO-WILD-TYPE CELLULAR RETINOICTITL 2 ACID BINDING PROTEIN II AT 1.4 A AND ITSTITL 3 RELATIONSHIP TO LIGAND BINDING AND NUCLEARTITL 4 TRANSLOCATION.REF J.MOL.BIOL. V. 363 687 2006REFN ISSN […]
General Structure Information 1kv3 TGM2 human tissue transglutaminase in gdp bound form 2.8Å AUTH S.LIU,R.A.CERIONE,J.CLARDYTITL STRUCTURAL BASIS FOR THE GUANINETITL 2 NUCLEOTIDE-BINDING ACTIVITY OF TISSUETITL 3 TRANSGLUTAMINASE AND ITS REGULATION OFTITL 4 TRANSAMIDATION ACTIVITY.REF PROC.NATL.ACAD.SCI.USA V. 99 2743 2002REFN ISSN 0027-8424PMID 11867708DOI 10.1073/PNAS.042454899 Variant Set Distributions Ripley’s K Analysis Plots Variant Set Comparisons Pathogenic Proximity […]
General Structure Information 3ij9 AMY2A directed in situ elongation as a strategy to characterize the covalent glycosyl-enzyme catalytic intermediate of human pancreatic a-amylase 1.85Å AUTH R.ZHANG,C.LI,L.K.WILLIAMS,B.P.REMPEL,G.D.BRAYER,AUTH 2 S.G.WITHERSTITL DIRECTED IN SITU INHIBITOR ELONGATION AS ATITL 2 STRATEGY TO STRUCTURALLY CHARACTERIZE THE COVALENTTITL 3 GLYCOSYL-ENZYME INTERMEDIATE OF HUMAN PANCREATICTITL 4 ALPHA-AMYLASEREF BIOCHEMISTRY V. 48 10752 2009REFN […]