Structure of PDB 8s32 Chain N Binding Site BS01

Receptor Information

>8s32 Chain N (length=525) Species: 562 (Escherichia coli)

AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLS
PYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIA
EDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQ
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH
ATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPL
RQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTR
SALQYAASVAGLMITTECMVTDLPK

Ligand information

>8s32 Chain 2 (length=12) Species: 32630 (synthetic construct)

SWMTTPWGFHLP

Receptor-Ligand Complex Structure

Structure summary

• PDB: 8s32 Depletion of essential GroEL protein in Escherichia coli using Clp-Interacting Peptidic Protein Erasers (CLIPPERs)
• Resolution: 2.45 Å
• Binding residue (original residue number in PDB): R230 L233 E237 T260 N264 I269
• Binding residue (residue number reindexed from 1): R230 L233 E237 T260 N264 I269

Enzymatic activity

• Enzyme Commision number: 5.6.1.7: chaperonin ATPase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0016853 isomerase activity
• GO:0016887 ATP hydrolysis activity
• GO:0042802 identical protein binding
• GO:0051082 unfolded protein binding
• GO:0140662 ATP-dependent protein folding chaperone

Biological Process

• GO:0006457 protein folding
• GO:0009314 response to radiation
• GO:0009408 response to heat
• GO:0019068 virion assembly
• GO:0042026 protein refolding
• GO:0051085 chaperone cofactor-dependent protein refolding

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0016020 membrane
• GO:1990220 GroEL-GroES complex

External links

• PDB: RCSB:8s32, PDBe:8s32, PDBj:8s32
• PDBsum: 8s32
• UniProt: P0A6F5|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)