Structure of PDB 4ab2 Chain F

Receptor sequence
>4ab2F (length=523) Species: 562 (Escherichia coli) [Search protein sequence]
AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLS
PYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIA
EDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQ
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEAALH
ATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPL
RQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTR
SALQYAASVAGLMITTECMVTDL
3D structure
PDB4ab2 ATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the Groel Chaperonin.
ChainF
Resolution8.5 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 A398
Catalytic site (residue number reindexed from 1) D51 T88 T89 A397
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 ATP F L31 G32 D87 G88 T89 T90 T91 I150 N153 G415 D495 L30 G31 D86 G87 T88 T89 T90 I149 N152 G414 D494
BS02 MG F D87 I150 D86 I149
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:4ab2, PDBe:4ab2, PDBj:4ab2
PDBsum4ab2
PubMed22445172
UniProtP0A6F5|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)

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