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 1dkd Chain C Binding Site BS01

Receptor Information
>1dkd Chain C (length=146) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAV
AKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQ
DIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGV
Ligand information
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]
PDB1dkd The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity.
Resolution2.1 Å
Binding residue
(original residue number in PDB)
I230 R231 L234 L237 E238 T261 N265 I270
Binding residue
(residue number reindexed from 1)
I40 R41 L44 L47 E48 T71 N75 I80
Enzymatic activity
Enzyme Commision number 5.6.1.7: chaperonin ATPase.
Gene Ontology
Molecular Function
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0042026 protein refolding

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1dkd, PDBe:1dkd, PDBj:1dkd
PDBsum1dkd
PubMed10619429
UniProtP0A6F5|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)

[Back to BioLiP]

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