Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1DO0

ORTHORHOMBIC CRYSTAL FORM OF HEAT SHOCK LOCUS U (HSLU) FROM ESCHERICHIA COLI

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004176	molecular_function	ATP-dependent peptidase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0009376	cellular_component	HslUV protease complex
A	0009408	biological_process	response to heat
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0019904	molecular_function	protein domain specific binding
A	0030164	biological_process	protein denaturation
A	0034605	biological_process	cellular response to heat
A	0036402	molecular_function	proteasome-activating activity
A	0042802	molecular_function	identical protein binding
A	0043335	biological_process	protein unfolding
A	0051603	biological_process	proteolysis involved in protein catabolic process
A	1901800	biological_process	positive regulation of proteasomal protein catabolic process
B	0000287	molecular_function	magnesium ion binding
B	0004176	molecular_function	ATP-dependent peptidase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0009376	cellular_component	HslUV protease complex
B	0009408	biological_process	response to heat
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0019904	molecular_function	protein domain specific binding
B	0030164	biological_process	protein denaturation
B	0034605	biological_process	cellular response to heat
B	0036402	molecular_function	proteasome-activating activity
B	0042802	molecular_function	identical protein binding
B	0043335	biological_process	protein unfolding
B	0051603	biological_process	proteolysis involved in protein catabolic process
B	1901800	biological_process	positive regulation of proteasomal protein catabolic process
C	0000287	molecular_function	magnesium ion binding
C	0004176	molecular_function	ATP-dependent peptidase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0009376	cellular_component	HslUV protease complex
C	0009408	biological_process	response to heat
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0019904	molecular_function	protein domain specific binding
C	0030164	biological_process	protein denaturation
C	0034605	biological_process	cellular response to heat
C	0036402	molecular_function	proteasome-activating activity
C	0042802	molecular_function	identical protein binding
C	0043335	biological_process	protein unfolding
C	0051603	biological_process	proteolysis involved in protein catabolic process
C	1901800	biological_process	positive regulation of proteasomal protein catabolic process
D	0000287	molecular_function	magnesium ion binding
D	0004176	molecular_function	ATP-dependent peptidase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0009376	cellular_component	HslUV protease complex
D	0009408	biological_process	response to heat
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0019904	molecular_function	protein domain specific binding
D	0030164	biological_process	protein denaturation
D	0034605	biological_process	cellular response to heat
D	0036402	molecular_function	proteasome-activating activity
D	0042802	molecular_function	identical protein binding
D	0043335	biological_process	protein unfolding
D	0051603	biological_process	proteolysis involved in protein catabolic process
D	1901800	biological_process	positive regulation of proteasomal protein catabolic process
E	0000287	molecular_function	magnesium ion binding
E	0004176	molecular_function	ATP-dependent peptidase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006508	biological_process	proteolysis
E	0008233	molecular_function	peptidase activity
E	0009376	cellular_component	HslUV protease complex
E	0009408	biological_process	response to heat
E	0016020	cellular_component	membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0019904	molecular_function	protein domain specific binding
E	0030164	biological_process	protein denaturation
E	0034605	biological_process	cellular response to heat
E	0036402	molecular_function	proteasome-activating activity
E	0042802	molecular_function	identical protein binding
E	0043335	biological_process	protein unfolding
E	0051603	biological_process	proteolysis involved in protein catabolic process
E	1901800	biological_process	positive regulation of proteasomal protein catabolic process
F	0000287	molecular_function	magnesium ion binding
F	0004176	molecular_function	ATP-dependent peptidase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006508	biological_process	proteolysis
F	0008233	molecular_function	peptidase activity
F	0009376	cellular_component	HslUV protease complex
F	0009408	biological_process	response to heat
F	0016020	cellular_component	membrane
F	0016887	molecular_function	ATP hydrolysis activity
F	0019904	molecular_function	protein domain specific binding
F	0030164	biological_process	protein denaturation
F	0034605	biological_process	cellular response to heat
F	0036402	molecular_function	proteasome-activating activity
F	0042802	molecular_function	identical protein binding
F	0043335	biological_process	protein unfolding
F	0051603	biological_process	proteolysis involved in protein catabolic process
F	1901800	biological_process	positive regulation of proteasomal protein catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 C 800

Chain	Residue
C	PRO58
C	GLY60
C	VAL61
C	GLY62
C	LYS63
C	THR64
C	ARG393

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 F 805

Chain	Residue
F	VAL61
F	GLY62
F	LYS63
F	THR64
F	ARG393
F	PRO58
F	GLY60

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 600

Chain	Residue
B	LYS63
B	ASP256
B	ATP905

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 605

Chain	Residue
E	LYS63
E	ASP256
E	ATP915

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP A 900

Chain	Residue
A	HIS16
A	ILE17
A	ILE18
A	PRO58
A	THR59
A	GLY60
A	VAL61
A	GLY62
A	LYS63
A	THR64
A	GLU65
A	LYS80
A	ASP256
A	LEU335
A	ALA392
A	ARG393
A	HIS396
B	GLU321

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP B 905

Chain	Residue
B	HIS16
B	ILE17
B	ILE18
B	PRO58
B	THR59
B	GLY60
B	VAL61
B	GLY62
B	LYS63
B	THR64
B	GLU65
B	LYS80
B	ASP256
B	SER307
B	LEU335
B	ILE343
B	ALA392
B	ARG393
B	HIS396
B	MG600
C	GLU321

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP D 910

Chain	Residue
D	HIS16
D	ILE17
D	ILE18
D	PRO58
D	THR59
D	GLY60
D	VAL61
D	GLY62
D	LYS63
D	THR64
D	GLU65
D	LYS80
D	ASP256
D	LEU335
D	ALA392
D	ARG393
D	HIS396
E	GLU321

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP E 915

Chain	Residue
E	HIS16
E	ILE17
E	ILE18
E	PRO58
E	THR59
E	GLY60
E	VAL61
E	GLY62
E	LYS63
E	THR64
E	GLU65
E	LYS80
E	ASP256
E	SER307
E	LEU335
E	ALA392
E	ARG393
E	MG605
F	GLU321

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	BINDING:

Chain	Residue	Details
A	ILE18
B	ARG393
C	ILE18
C	GLY60
C	ASP256
C	GLU321
C	ARG393
D	ILE18
D	GLY60
D	ASP256
D	GLU321
A	GLY60
D	ARG393
E	ILE18
E	GLY60
E	ASP256
E	GLU321
E	ARG393
F	ILE18
F	GLY60
F	ASP256
F	GLU321
A	ASP256
F	ARG393
A	GLU321
A	ARG393
B	ILE18
B	GLY60
B	ASP256
B	GLU321

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1nsf

Chain	Residue	Details
A	LYS140
A	LYS240
A	LYS63

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1nsf

Chain	Residue	Details
B	LYS140
B	LYS240
B	LYS63

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1nsf

Chain	Residue	Details
C	LYS140
C	LYS240
C	LYS63

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1nsf

Chain	Residue	Details
D	LYS140
D	LYS240
D	LYS63

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1nsf

Chain	Residue	Details
E	LYS140
E	LYS240
E	LYS63

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1nsf

Chain	Residue	Details
F	LYS140
F	LYS240
F	LYS63

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)