2Q8K.A | PA2G4

General Structure Information 2q8k PA2G4 the crystal structure of ebp1 1.6Å AUTH E.KOWALINSKI,G.BANGE,B.BRADATSCH,E.HURT,K.WILD,I.SINNINGTITL THE CRYSTAL STRUCTURE OF EBP1 REVEALS A METHIONINETITL 2 AMINOPEPTIDASE FOLD AS BINDING PLATFORM FOR MULTIPLETITL 3 INTERACTIONS.REF FEBS LETT. V. 581 4450 2007REFN ISSN 0014-5793PMID 17765895DOI 10.1016/J.FEBSLET.2007.08.024 Variant Set Distributions Ripley’s K Analysis Plots Variant Set Comparisons Pathogenic Proximity Analysis Mapped […]

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3JYH.A | DPP7

General Structure Information 3jyh DPP7 human dipeptidyl peptidase dpp7 2.19Å AUTH E.DOBROVETSKY,A.DONG,A.SEITOVA,L.CROMBETT,S.PAGANON,AUTH 2 D.COSSAR,A.M.EDWARDS,C.H.ARROWSMITH,C.BOUNTRA,J.WEIGELT,AUTH 3 A.HASSEL,L.SHEWCHUK,A.BOCHKAREVTITL HUMAN DIPEPTIDYL PEPTIDASE DPP7REF TO BE PUBLISHEDREFN Variant Set Distributions Ripley’s K Analysis Plots Variant Set Comparisons Mapped Variants

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3MDJ.C | ERAP1

General Structure Information 3mdj ERAP1 er aminopeptidase, erap1, bound to the zinc aminopeptidase inhibitor, bestatin 2.95Å AUTH T.T.NGUYEN,S.C.CHANG,I.EVNOUCHIDOU,I.A.YORK,C.ZIKOS,AUTH 2 K.L.ROCK,A.L.GOLDBERG,E.STRATIKOS,L.J.STERNTITL STRUCTURAL BASIS FOR ANTIGENIC PEPTIDE PRECURSOR PROCESSINGTITL 2 BY THE ENDOPLASMIC RETICULUM AMINOPEPTIDASE ERAP1.REF NAT.STRUCT.MOL.BIOL. V. 18 604 2011REFN ISSN 1545-9993PMID 21478864DOI 10.1038/NSMB.2021 Variant Set Distributions Ripley’s K Analysis Plots Variant Set Comparisons Mapped Variants

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3CTZ.A | XPNPEP1

General Structure Information 3ctz XPNPEP1 structure of human cytosolic x-prolyl aminopeptidase 1.6Å AUTH X.LI,Z.LOU,X.LI,W.ZHOU,M.MA,Y.CAO,Y.GENG,M.BARTLAM,AUTH 2 X.C.ZHANG,Z.RAOTITL STRUCTURE OF HUMAN CYTOSOLIC X-PROLYL AMINOPEPTIDASE: ATITL 2 DOUBLE MN(II)-DEPENDENT DIMERIC ENZYME WITH A NOVELTITL 3 THREE-DOMAIN SUBUNITREF J.BIOL.CHEM. V. 283 22858 2008REFN ISSN 0021-9258PMID 18515364DOI 10.1074/JBC.M710274200 Variant Set Distributions Ripley’s K Analysis Plots Variant Set Comparisons Mapped Variants

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4E36.A | ERAP2

General Structure Information 4e36 ERAP2 crystal structure of the human endoplasmic reticulum aminopeptidase 2 variant n392k 3.22Å AUTH I.EVNOUCHIDOU,J.BIRTLEY,S.SEREGIN,A.PAPAKYRIAKOU,E.ZERVOUDI,AUTH 2 M.SAMIOTAKI,G.PANAYOTOU,P.GIASTAS,O.PETRAKIS,D.GEORGIADIS,AUTH 3 A.AMALFITANO,E.SARIDAKIS,I.M.MAVRIDIS,E.STRATIKOSTITL A COMMON SINGLE NUCLEOTIDE POLYMORPHISM IN ENDOPLASMICTITL 2 RETICULUM AMINOPEPTIDASE 2 INDUCES A SPECIFICITY SWITCH THATTITL 3 LEADS TO ALTERED ANTIGEN PROCESSING.REF J.IMMUNOL. V. 189 2383 2012REFN ISSN 0022-1767PMID 22837489DOI 10.4049/JIMMUNOL.1200918 Variant […]

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1CB5.C | BLMH

General Structure Information 1cb5 BLMH human bleomycin hydrolase. 2.59Å AUTH P.A.OFARRELL,F.GONZALEZ,W.ZHENG,S.A.JOHNSTON,L.JOSHUA-TORTITL CRYSTAL STRUCTURE OF HUMAN BLEOMYCIN HYDROLASE, ATITL 2 SELF-COMPARTMENTALIZING CYSTEINE PROTEASE.REF STRUCTURE FOLD.DES. V. 7 619 1999REFN ISSN 0969-2126PMID 10404591DOI 10.1016/S0969-2126(99)80083-5 Variant Set Distributions Ripley’s K Analysis Plots Variant Set Comparisons Pathogenic Proximity Analysis Mapped Variants

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4IKU.A | METAP1

General Structure Information 4iku METAP1 crystal structure of truncated (delta 1-89) human methionine aminopeptidase type 1 in complex with 2-((5-chloro-6-methyl-2- (pyridin-2-yl)pyrimidin-4-yl)amino)-3-phenylpropanamide 1.3Å AUTH C.KISHOR,T.ARYA,R.REDDI,X.CHEN,V.SADDANAPU,A.K.MARAPAKA,AUTH 2 R.GUMPENA,D.MA,J.O.LIU,A.ADDLAGATTATITL IDENTIFICATION, BIOCHEMICAL AND STRUCTURAL EVALUATION OFTITL 2 SPECIES-SPECIFIC INHIBITORS AGAINST TYPE I METHIONINETITL 3 AMINOPEPTIDASESREF J.MED.CHEM. V. 56 5295 2013REFN ISSN 0022-2623PMID 23767698DOI 10.1021/JM400395P Variant Set Distributions Ripley’s K […]

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1NB3.I | CSTA

General Structure Information 1nb3 CSTA crystal structure of stefin a in complex with cathepsin h: n-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases 2.8Å AUTH S.JENKO,I.DOLENC,G.GUNCAR,A.DOBERSEK,M.PODOBNIK,D.TURKTITL CRYSTAL STRUCTURE OF STEFIN A IN COMPLEX WITH CATHEPSIN H:TITL 2 N-TERMINAL RESIDUES OF INHIBITORS CAN ADAPT TO THE ACTIVETITL 3 SITES OF ENDO- […]

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