Structure of PDB 2ynj Chain B

Receptor sequence

>2ynjB (length=524) Species: 364106 (Escherichia coli UTI89)

AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLS
PYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIA
EDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQ
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH
ATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPL
RQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTR
SALQYAASVAGLMITTECMVTDLP

3D structure

• PDB: 2ynj Protein Secondary Structure Determination by Constrained Single-Particle Cryo-Electron Tomography
• Chain: B
• Resolution: 8.4 Å

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	AGS	B	G32 P33 D87 G88 T89 T90 T91 G414 G415 N479 A480 A481 I493 D495	G31 P32 D86 G87 T88 T89 T90 G413 G414 N478 A479 A480 I492 D494

Gene Ontology

Molecular Function

• GO:0005524 ATP binding
• GO:0016853 isomerase activity
• 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

External links

• PDB: RCSB:2ynj, PDBe:2ynj, PDBj:2ynj
• PDBsum: 2ynj
• PubMed: 23217682
• UniProt: Q1R3B6|CH60_ECOUT Chaperonin GroEL (Gene Name=groEL)