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 1y79 Chain 1

Receptor sequence
>1y791 (length=680) Species: 562 (Escherichia coli) [Search protein sequence]
TTMNPFLVQSTLPYLAPHFDQIANHHYRPAFDEGMQQKRAEIAAIALNPQ
MPDFNNTILALEQSGELLTRVTSVFFAMTAAHTNDELQRLDEQFSAELAE
LANDIYLNGELFARVDAVWQRRESLGLDSESIRLVEVIHQRFVLAGAKLA
QADKAKLKVLNTEAATLTSQFNQRLLAANKSGGLVVNDIAQLAGMSEQEI
ALAAEAAREKGLDNKWLIPLLNTTQQPALAEMRDRATREKLFIAGWTRAE
KNDANDTRAIIQRLVEIRAQQATLLGFPHYAAWKIADQMAKTPEAALNFM
REIVPAARQRASDELASIQAVIDKQQGGFSAQPWDWAFYAEQVRREKFDL
DEAQLKPYFELNTVLNEGVFWTANQLFGIKFVERFDIPVYHPDVRVWEIF
DHNGVGLALFYGDFFARDSKSGGAWMGNFVEQSTLNKTHPVIYNVCNYQK
PAAGEPALLLWDDVITLFHEFGHTLHGLFARQRYATLSGTNTPRDFVEFP
SQINEHWATHPQVFARYARHYQSGAAMPDELQQKMRNASLFNKGYEMSEL
LSAALLDMRWHCLEENEAMQDVDDFELRALVAENMDLPAIPPRYRSSYFA
HIFGGGYAAGYYAYLWTQMLADDGYQWFVEQGGLTRENGLRFREAILSRG
NSEDLERLYRQWRGKAPKIMPMLQHRGLNI
3D structure
PDB1y79 Crystal Structure of the E.coli Dipeptidyl Carboxypeptidase Dcp: Further Indication of a Ligand-dependant Hinge Movement Mechanism
Chain1
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H469 E470 H473
Catalytic site (residue number reindexed from 1) H469 E470 H473
Enzyme Commision number 3.4.15.5: peptidyl-dipeptidase Dcp.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN 1 H469 H473 E498 H469 H473 E498
BS02 LYS 1 W425 M426 G606 Y607 W425 M426 G606 Y607
BS03 TRP 1 A424 H469 E470 H473 E498 A600 H601 G605 Y607 Y614 A424 H469 E470 H473 E498 A600 H601 G605 Y607 Y614
BS04 GLY 1 H469 H601 H469 H601
BS05 ASP 1 R593 Y594 Y611 Y614 R593 Y594 Y611 Y614
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0030288 outer membrane-bounded periplasmic space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1y79, PDBe:1y79, PDBj:1y79
PDBsum1y79
PubMed15876371
UniProtP24171|DCP_ECOLI Dipeptidyl carboxypeptidase (Gene Name=dcp)

[Back to BioLiP]

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