BioLiP

Receptor Information

>1kp8 Chain D (length=525) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

AAKDVKFGNDAGVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITK
DGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIIT
EGLKAVAAGMNPMDLKRGIDKAVTVAVEELKALSVPCSDSKAIAQVGTIS
ANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLS
PYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIA
EDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQ
QIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALH
ATRAAVEEGVVAGGGVALIRVASKLADLRGQNADQNVGIKVALRAMEAPL
RQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTR
SALQYAASVAGLMITTECMVTDLPK

Ligand ID

AGS

InChI

InChI=1S/C10H16N5O12P3S/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(25-10)1-24-28(18,19)26-29(20,21)27-30(22,23)31/h2-4,6-7,10,16-17H,1H2,(H,18,19)(H,20,21)(H2,11,12,13)(H2,22,23,31)/t4-,6-,7-,10-/m1/s1

InChIKey

NLTUCYMLOPLUHL-KQYNXXCUSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.7.6	c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=S)(O)O)O)O)N
CACTVS 3.370	Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=S)[C@@H](O)[C@H]3O
CACTVS 3.370	Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=S)[CH](O)[CH]3O
OpenEye OEToolkits 1.7.6	c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)OP(=O)(O)OP(=S)(O)O)O)O)N
ACDLabs 12.01	O=P(O)(OP(=S)(O)O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O

Formula

C10 H16 N5 O12 P3 S

Name

PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER;
ATP-GAMMA-S;
ADENOSINE 5'-(3-THIOTRIPHOSPHATE);
ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE);
ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE

PDB chain

1kp8 Chain D Residue 551 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1kp8 Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution
Resolution	2.0 Å
Binding residue (original residue number in PDB)	L31 G32 P33 G53 D87 G88 T89 T90 T91 G414 G415 N479 A480 I493 D495
Binding residue (residue number reindexed from 1)	L30 G31 P32 G52 D86 G87 T88 T89 T90 G413 G414 N478 A479 I492 D494
Annotation score	4

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.

	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

PDB	RCSB:1kp8, PDBe:1kp8, PDBj:1kp8
PDBsum	1kp8
PubMed	12654267
UniProt	P0A6F5\|CH60_ECOLI Chaperonin GroEL (Gene Name=groEL)

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Structure of PDB 1kp8 Chain D Binding Site BS01