Structure of PDB 5opx Chain A

Receptor sequence
>5opxA (length=520) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVACGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVMQFDRGYLSPY
FINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAED
VEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISE
EIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQI
EEATSDYDREKLQERVAKLAVAVIKVGAATEVEMKEKKARVEDALHATRA
AVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIV
LNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTRSALQ
YAASVAGLMITTECMVTDLP
3D structure
PDB5opx GroEL Ring Separation and Exchange in the Chaperonin Reaction.
ChainA
Resolution3.64 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D52 T89 T90 D398
Catalytic site (residue number reindexed from 1) D51 T88 T89 D393
Enzyme Commision number 5.6.1.7: chaperonin ATPase.
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 ADP A L31 G32 P33 D87 G88 T89 T90 T91 I150 G414 G415 I454 N479 A480 A481 I493 D495 L30 G31 P32 D86 G87 T88 T89 T90 I149 G409 G410 I449 N474 A475 A476 I488 D490
BS02 BEF A D52 D87 T89 D398 D51 D86 T88 D393
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5opx, PDBe:5opx, PDBj:5opx
PDBsum5opx
PubMed29336887
UniProtP0A6F5|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)

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