Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KI8

Crystal structure of a GroEL-ADP complex in the relaxed allosteric state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006457	biological_process	protein folding
A	0009408	biological_process	response to heat
A	0016853	molecular_function	isomerase activity
A	0042026	biological_process	protein refolding
A	0046872	molecular_function	metal ion binding
A	0051082	molecular_function	unfolded protein binding
A	0051085	biological_process	chaperone cofactor-dependent protein refolding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
A	1990220	cellular_component	GroEL-GroES complex
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006457	biological_process	protein folding
B	0009408	biological_process	response to heat
B	0016853	molecular_function	isomerase activity
B	0042026	biological_process	protein refolding
B	0046872	molecular_function	metal ion binding
B	0051082	molecular_function	unfolded protein binding
B	0051085	biological_process	chaperone cofactor-dependent protein refolding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
B	1990220	cellular_component	GroEL-GroES complex
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006457	biological_process	protein folding
C	0009408	biological_process	response to heat
C	0016853	molecular_function	isomerase activity
C	0042026	biological_process	protein refolding
C	0046872	molecular_function	metal ion binding
C	0051082	molecular_function	unfolded protein binding
C	0051085	biological_process	chaperone cofactor-dependent protein refolding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
C	1990220	cellular_component	GroEL-GroES complex
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006457	biological_process	protein folding
D	0009408	biological_process	response to heat
D	0016853	molecular_function	isomerase activity
D	0042026	biological_process	protein refolding
D	0046872	molecular_function	metal ion binding
D	0051082	molecular_function	unfolded protein binding
D	0051085	biological_process	chaperone cofactor-dependent protein refolding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
D	1990220	cellular_component	GroEL-GroES complex
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0006457	biological_process	protein folding
E	0009408	biological_process	response to heat
E	0016853	molecular_function	isomerase activity
E	0042026	biological_process	protein refolding
E	0046872	molecular_function	metal ion binding
E	0051082	molecular_function	unfolded protein binding
E	0051085	biological_process	chaperone cofactor-dependent protein refolding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
E	1990220	cellular_component	GroEL-GroES complex
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0006457	biological_process	protein folding
F	0009408	biological_process	response to heat
F	0016853	molecular_function	isomerase activity
F	0042026	biological_process	protein refolding
F	0046872	molecular_function	metal ion binding
F	0051082	molecular_function	unfolded protein binding
F	0051085	biological_process	chaperone cofactor-dependent protein refolding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
F	1990220	cellular_component	GroEL-GroES complex
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0006457	biological_process	protein folding
G	0009408	biological_process	response to heat
G	0016853	molecular_function	isomerase activity
G	0042026	biological_process	protein refolding
G	0046872	molecular_function	metal ion binding
G	0051082	molecular_function	unfolded protein binding
G	0051085	biological_process	chaperone cofactor-dependent protein refolding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
G	1990220	cellular_component	GroEL-GroES complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ADP A 601

Chain	Residue
A	THR30
A	GLY415
A	TYR478
A	ASN479
A	ALA480
A	ILE493
A	ASP495
A	MG602
A	K603
A	HOH710
A	HOH711
A	LEU31
A	HOH716
A	HOH728
A	HOH750
A	HOH768
A	GLY32
A	ASP87
A	GLY88
A	THR89
A	THR90
A	THR91
A	GLY414

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 602

Chain	Residue
A	ASP87
A	ADP601
A	HOH710
A	HOH716
A	HOH750

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K A 603

Chain	Residue
A	THR30
A	LYS51
A	ADP601
A	HOH720
A	HOH742
A	HOH768
A	HOH770

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD A 604

Chain	Residue
A	GLU191
A	GLN343
A	ALA373
A	HOH778

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 605

Chain	Residue
A	ASN10
A	VAL14
A	LEU17
A	LEU104
A	ALA108

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD A 606

Chain	Residue
A	GLU518
G	LEU456
G	ASN457

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD A 607

Chain	Residue
A	GLN505
A	HOH789

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 608

Chain	Residue
A	ARG36
A	GLN453
A	LEU456
A	ASN457
B	GLU518

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MPD A 609

Chain	Residue
A	ALA84
A	ALA85
A	GLY86
A	HIS401
A	ARG404
A	GLU408
A	LYS498

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 610

Chain	Residue
A	LYS42
A	SER43
B	HOH750
B	HOH756

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CA A 611

Chain	Residue
A	ARG445

site_id	BC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ADP B 601

Chain	Residue
B	THR30
B	LEU31
B	GLY32
B	PRO33
B	ASP87
B	GLY88
B	THR89
B	THR90
B	THR91
B	GLY414
B	GLY415
B	TYR478
B	ASN479
B	ALA480
B	ALA481
B	ILE493
B	ASP495
B	MG602
B	K603
B	HOH711
B	HOH733
B	HOH753
B	HOH758
B	HOH761

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 602

Chain	Residue
B	ASP87
B	ADP601
B	HOH753
B	HOH757
B	HOH758

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 603

Chain	Residue
B	HOH783
B	HOH784
B	THR30
B	LYS51
B	ADP601
B	HOH782

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD B 604

Chain	Residue
B	VAL14
B	LEU104
B	LYS105
B	ALA108
B	HOH776

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD B 605

Chain	Residue
B	ARG36
B	LEU456
B	ASN457
B	HOH787
C	GLU518

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD B 607

Chain	Residue
B	GLU102
B	ARG445

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD B 608

Chain	Residue
B	ALA83
B	ALA84
B	GLY86
B	HIS401
B	GLU408
B	LYS498

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 609

Chain	Residue
B	GLU460
B	HOH778
B	HOH790
C	HOH771

site_id	CC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP C 601

Chain	Residue
C	THR30
C	LEU31
C	GLY32
C	PRO33
C	ASP87
C	GLY88
C	THR89
C	THR90
C	THR91
C	GLY414
C	GLY415
C	TYR478
C	ASN479
C	ALA480
C	ALA481
C	ILE493
C	ASP495
C	MG602
C	K603
C	HOH721
C	HOH722
C	HOH736
C	HOH737
C	HOH743
C	HOH766
C	HOH781

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 602

Chain	Residue
C	ASP87
C	ADP601
C	HOH736
C	HOH741
C	HOH749
C	HOH781

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 603

Chain	Residue
C	THR30
C	GLY32
C	LYS51
C	ADP601
C	HOH721
C	HOH766

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD C 604

Chain	Residue
C	VAL14
C	LEU104
C	ALA108
C	HOH775

site_id	CC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP D 601

Chain	Residue
D	THR30
D	LEU31
D	GLY32
D	PRO33
D	ASP87
D	GLY88
D	THR89
D	THR90
D	THR91
D	ILE150
D	GLY414
D	GLY415
D	TYR478
D	ASN479
D	ALA480
D	ALA481
D	ILE493
D	ASP495
D	MG602
D	K603
D	HOH709
D	HOH738
D	HOH756
D	HOH757
D	HOH766
D	HOH784

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 602

Chain	Residue
D	ASP87
D	ADP601
D	HOH709
D	HOH738
D	HOH756

site_id	CC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE K D 603

Chain	Residue
D	THR30
D	LYS51
D	ASN153
D	ADP601
D	HOH766
D	HOH767
D	HOH768
D	HOH783

site_id	CC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD D 604

Chain	Residue
D	ASN10
D	VAL14
D	LEU17
D	LEU104
D	LYS105
D	HOH770

site_id	DC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD D 605

Chain	Residue
D	ILE175
D	THR176

site_id	DC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MPD D 606

Chain	Residue
D	ASP25

site_id	DC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 607

Chain	Residue
C	HOH742
C	HOH756
C	HOH774
C	HOH784
D	HOH713

site_id	DC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ADP E 601

Chain	Residue
E	THR30
E	LEU31
E	GLY32
E	PRO33
E	ASP87
E	GLY88
E	THR89
E	THR90
E	THR91
E	GLY414
E	GLY415
E	TYR478
E	ASN479
E	ALA480
E	ALA481
E	ILE493
E	ASP495
E	MG602
E	K603
E	HOH714
E	HOH720
E	HOH731
E	HOH737
E	HOH738
E	HOH747

site_id	DC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 602

Chain	Residue
E	ASP87
E	ADP601
E	HOH731
E	HOH737
E	HOH738

site_id	DC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K E 603

Chain	Residue
E	THR30
E	GLY32
E	ADP601
E	HOH712
E	HOH713
E	HOH714

site_id	DC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD E 604

Chain	Residue
E	GLU102
E	ARG445

site_id	DC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA E 605

Chain	Residue
D	HOH778
E	LYS65
E	HOH735

site_id	DC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA E 606

Chain	Residue
E	SER43
E	HOH727
E	HOH761

site_id	EC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CA E 607

Chain	Residue
E	HOH756

site_id	EC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP F 601

Chain	Residue
F	THR30
F	LEU31
F	GLY32
F	PRO33
F	ASP87
F	GLY88
F	THR89
F	THR90
F	THR91
F	ILE150
F	ASN153
F	GLY414
F	GLY415
F	TYR478
F	ASN479
F	ALA480
F	ALA481
F	ILE493
F	ASP495
F	MG602
F	K603
F	HOH706
F	HOH707
F	HOH723
F	HOH737
F	HOH754

site_id	EC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 602

Chain	Residue
F	ASP87
F	ADP601
F	HOH706
F	HOH707
F	HOH723

site_id	EC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K F 603

Chain	Residue
F	THR30
F	LYS51
F	ADP601
F	HOH743
F	HOH744
F	HOH745

site_id	EC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD F 604

Chain	Residue
F	THR176
F	VAL324
F	THR331

site_id	EC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K F 605

Chain	Residue
F	GLU460
F	GLU483
F	HOH759

site_id	EC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP G 601

Chain	Residue
G	THR30
G	LEU31
G	GLY32
G	PRO33
G	ASP87
G	GLY88
G	THR89
G	THR90
G	THR91
G	GLY414
G	GLY415
G	TYR478
G	ASN479
G	ALA480
G	ALA481
G	ILE493
G	ASP495
G	MG602
G	K603
G	HOH706
G	HOH712
G	HOH729
G	HOH733
G	HOH761
G	HOH762
G	HOH779

site_id	EC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG G 602

Chain	Residue
G	ASP87
G	ADP601
G	HOH706
G	HOH729
G	HOH733

site_id	EC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K G 603

Chain	Residue
G	THR30
G	LYS51
G	ADP601
G	HOH762
G	HOH763
G	HOH765
G	HOH766

site_id	FC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD G 604

Chain	Residue
G	LEU17
G	LEU104
G	LYS105
G	ALA108
G	HOH736
G	HOH748

site_id	FC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MPD G 605

Chain	Residue
G	TYR506

site_id	FC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CA G 606

Chain	Residue
A	HOH714
G	SER43

site_id	FC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CA G 607

Chain	Residue
G	ARG445

site_id	FC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE K G 608

Chain	Residue
G	GLU460
G	GLU483

site_id	FC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA G 609

Chain	Residue
A	PRO113
A	HOH734
G	ARG36
G	HOH725

Functional Information from PROSITE/UniProt

site_id	PS00296
Number of Residues	12
Details	CHAPERONINS_CPN60 Chaperonins cpn60 signature. AAVEEGVVaGGG

Chain	Residue	Details
A	ALA405-GLY416

site_id	PS01034
Number of Residues	12
Details	GH16_1 Glycosyl hydrolases family 16 active sites. ELDVvEgmQFdA

Chain	Residue	Details
A	GLU186-ALA197

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)