Structure of PDB 4pko Chain L

Receptor sequence
>4pkoL (length=524) Species: 562 (Escherichia coli) [Search protein sequence]
AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLS
PYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIA
EDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQ
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH
ATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPL
RQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTR
SALQYAASVAGLMITTECMVTDLP
3D structure
PDB4pko Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form.
ChainL
Resolution3.84 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 D397
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 L L31 G32 P33 K51 D87 G88 T90 T91 G414 G415 I454 N479 A480 I493 D495 L30 G31 P32 K50 D86 G87 T89 T90 G413 G414 I453 N478 A479 I492 D494
BS02 BEF L D52 G53 D87 G88 T89 T90 D398 D51 G52 D86 G87 T88 T89 D397
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016853 isomerase activity
GO:0046872 metal ion binding
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0009408 response to heat
GO:0042026 protein refolding
GO:0051085 chaperone cofactor-dependent protein refolding
Cellular Component
GO:0005737 cytoplasm
GO:1990220 GroEL-GroES complex

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Cellular Component
External links
PDB RCSB:4pko, PDBe:4pko, PDBj:4pko
PDBsum4pko
PubMed25136110
UniProtQ548M1

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