Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

BioLiP

Structure of PDB 7mey Chain A Binding Site BS03

Receptor Information
>7mey Chain A (length=1731) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSLQGHIRRTLRSIHNLPYFRYTRGPTERADMSRALKEFIYRYLYFVISN
SGENLPTLFNAHPKQKLLTVFPDSLEDAVDIDKITSQQTIPFYKIDESRI
GDVHKHTGRNCGRKFKIGEPLYRCHECGCDDTCVLCIHCFNPKDHVNHHV
CTDICTEFTSGICDCGDEEAWNSPLHCKAEEQEDVWNDSVNIALVELVLA
EVFDYFIDVFNQNIEPLPTIQKDITIKLREMTQQGKMYERAQFLNDLKYE
NDYKIDPENYTVIIYNDEYHNYSQATTALRQGVPDNVHIDLLTSRIDGEG
RAMLKCSQDLSSVLGGFFAVQTNGLSATLTSWSEYLHQETCKYIILWITH
CLNIPNSSFQTTFRNMMGKTLCSEYLNATECRDMTPVVEKYFSNKFDKND
PYRYIDLSILADGNQIPLGHHKILPESSTHSLSPLINDVETPTSRTYSNT
RLQHILYFDNRYWKRLRKDIQNVIIPTLASSNLYKPIFCQQVVEIFNHIT
RSVAYMDREPQLTAIRECVVQLFTCPTNAKNIFENQSFLDIVWSIIDIFK
EFCKVEGGVLIWQRVQKSNLTKSYSISFKQGLYTVETLLSKVHDPNIPLR
PKEIISLLTLCKLFNGAWKIKRKEGEHVLHEDQNFISYLEYTTSIYSIIQ
TAEKVSEKSKDSIDSKLFLNAIRIISSFLGNRSLTYKLIYDSHEVIKFSV
SHERVAFMNPLQTMLSFLIEKVSLKDAYEALEDCSDFLKISDFSLRSVVL
CSQIDVGFWVRNGMSVLHQASYYKNNPELGSYSRDIHLNQLAILWERDDI
PRIIYNILDRWELLDWFTGEVDYQHTVYEDKISFIIQQFIAFIYQILTER
QYFKTFSSLKDRRMDQIKNSIIYNLYMKPLSYSKLLRSVPDYLTEDTTEF
DEALEEVSVFVEPKGLADNGVFKLKASLYAKVDPLKLLNLENEFESSATI
IKSHLAKDKDEIAKVVLIPQVSIKQLDKDALNLGAFTRNTVFAKVVYKLL
QVCLDMEDSTFLNELLHLVHGIFRDDELINGKDSIPEAYLSKPICNLLLS
IANAKSDVFSESIVRKADYLLEKMIMKKPNELFESLIASFGNQYVNDYKD
KKLRTEKERKRRLAKKHQARLLAKFNNQQTKFMKEHFTCALCQDSSSTDF
FVIPAYHDHSPIFRPGNIFNPNEFMPMWDGFYNDDEKQAYIDDDVLEALK
ENGSCGSRKVFVSCNHHIHHNCFKRYVQKKRFSSNAFICPLCQTFSNCTL
PLCQTSKANTGLSLDMFLESELSLDTLSRLFKPFTEENYRTINSIFSLMI
SQCQGFDKAVRKRANFSHKDVSLILSVHWANTISMLEIASRLEKPYSISF
FRSREQKYKTLKNILVCIMLFTFVIGKPSMEFEPYPQQPDTVWNQNQLFQ
YIVRSALFSPVSLRQTVTEALTTFSRQFLRDFLQGLSDAEQVTKLYAKAS
KIGDVLKVSEQMLFALRTISDVRMEGLDSESIIYDLAYTFLLKSLLPTIR
RCLVFIKVLHELVKDSENETLVINGHEVEEELEFEDTAEFVNKALKMITE
KESLVDLLTTQESIVSHPYLENIPYEYCGIIKLIDLSKYLNTYVTQSKEI
KLREERSQHMKNADNRLDFKICLTCGVKVHLRADRHEMTKHLNKNCFKPF
GAFLMPNSSEVCLHLTQPPSNIFISAPYLNSHGEVGRNAMRRGDLTTLNL
KRYEHLNRLWINNEIPGYISRVMGDEFRVTI
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain7mey Chain A Residue 2002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB7mey Structural insights into Ubr1-mediated N-degron polyubiquitination.
Resolution3.67 Å
Binding residue
(original residue number in PDB)		C123 C148 C151 C175
Binding residue
(residue number reindexed from 1)		C111 C136 C139 C163
Annotation score4
Enzymatic activity
Enzyme Commision number 2.3.2.27: RING-type E3 ubiquitin transferase.
Gene Ontology
Molecular Function
GO:0004842 ubiquitin-protein transferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0061630 ubiquitin protein ligase activity
GO:1904855 proteasome regulatory particle binding
Biological Process
GO:0000209 protein polyubiquitination
GO:0006513 protein monoubiquitination
GO:0016567 protein ubiquitination
GO:0034620 cellular response to unfolded protein
GO:0036503 ERAD pathway
GO:0071596 ubiquitin-dependent protein catabolic process via the N-end rule pathway
GO:0071629 cytoplasm protein quality control by the ubiquitin-proteasome system
GO:0072671 mitochondria-associated ubiquitin-dependent protein catabolic process
GO:0090089 regulation of dipeptide transport
GO:0120174 stress-induced homeostatically regulated protein degradation pathway
GO:1990116 ribosome-associated ubiquitin-dependent protein catabolic process
Cellular Component
GO:0000151 ubiquitin ligase complex
GO:0005737 cytoplasm
GO:0008540 proteasome regulatory particle, base subcomplex
GO:1990303 UBR1-RAD6 ubiquitin ligase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7mey, PDBe:7mey, PDBj:7mey
PDBsum7mey
PubMed34789879
UniProtP19812|UBR1_YEAST E3 ubiquitin-protein ligase UBR1 (Gene Name=UBR1)

[Back to BioLiP]

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417