Structure of PDB 4pko Chain I

Receptor sequence
>4pkoI (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.
ChainI
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 I G32 P33 K51 D87 G88 T91 G414 G415 I454 N479 A480 I493 D495 G31 P32 K50 D86 G87 T90 G413 G414 I453 N478 A479 I492 D494
BS02 BEF I G53 D87 G88 T89 T90 G52 D86 G87 T88 T89
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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