Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1G4A

CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM

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	0004298	molecular_function	threonine-type endopeptidase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005839	cellular_component	proteasome core complex
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	0019904	molecular_function	protein domain specific binding
A	0030163	biological_process	protein catabolic process
A	0030164	biological_process	protein denaturation
A	0034605	biological_process	cellular response to heat
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0051603	biological_process	proteolysis involved in protein catabolic process
B	0000287	molecular_function	magnesium ion binding
B	0004176	molecular_function	ATP-dependent peptidase activity
B	0004298	molecular_function	threonine-type endopeptidase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005839	cellular_component	proteasome core complex
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	0019904	molecular_function	protein domain specific binding
B	0030163	biological_process	protein catabolic process
B	0030164	biological_process	protein denaturation
B	0034605	biological_process	cellular response to heat
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0051603	biological_process	proteolysis involved in protein catabolic process
C	0000287	molecular_function	magnesium ion binding
C	0004176	molecular_function	ATP-dependent peptidase activity
C	0004298	molecular_function	threonine-type endopeptidase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005839	cellular_component	proteasome core complex
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	0019904	molecular_function	protein domain specific binding
C	0030163	biological_process	protein catabolic process
C	0030164	biological_process	protein denaturation
C	0034605	biological_process	cellular response to heat
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0051603	biological_process	proteolysis involved in protein catabolic process
D	0000287	molecular_function	magnesium ion binding
D	0004176	molecular_function	ATP-dependent peptidase activity
D	0004298	molecular_function	threonine-type endopeptidase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005839	cellular_component	proteasome core complex
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	0019904	molecular_function	protein domain specific binding
D	0030163	biological_process	protein catabolic process
D	0030164	biological_process	protein denaturation
D	0034605	biological_process	cellular response to heat
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0051603	biological_process	proteolysis involved in 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	12
Details	BINDING SITE FOR RESIDUE DAT E 905

Chain	Residue
E	HIS16
E	ILE343
E	ALA392
E	ARG393
E	ILE17
E	ILE18
E	GLY60
E	VAL61
E	GLY62
E	LYS63
E	THR64
E	GLU65

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DAT F 906

Chain	Residue
F	ILE17
F	ILE18
F	THR59
F	GLY60
F	VAL61
F	GLY62
F	LYS63
F	THR64
F	GLU65
F	ILE343
F	ARG393

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00248, ECO:0000269\|PubMed:9257689

Chain	Residue	Details
B	THR2
F	ARG393
A	THR2
D	THR2
C	THR2
E	ARG393
F	ILE18
F	GLY60
F	ASP256
F	GLU321

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
B	ASP157
C	ASP157
C	ILE160
C	ASN163
B	ILE160
B	ASN163
A	ASP157
A	ILE160
A	ASN163
D	ASP157
D	ILE160
D	ASN163

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
B	GLY48
B	LYS33
B	THR1
B	SER124

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
F	LYS63
F	LYS240

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
A	GLY48
A	LYS33
A	THR1
A	SER124

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
D	GLY48
D	LYS33
D	THR1
D	SER124

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
C	GLY48
C	LYS33
C	THR1
C	SER124

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
B	GLY45
B	LYS33
B	THR1
B	SER124

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
A	GLY45
A	LYS33
A	THR1
A	SER124

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
D	GLY45
D	LYS33
D	THR1
D	SER124

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
C	GLY45
C	LYS33
C	THR1
C	SER124

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
E	LYS63
E	LYS240

site_id	MCSA1
Number of Residues	4
Details	M-CSA 678

Chain	Residue	Details
B	THR2	proton acceptor, proton donor
B	VAL34	electrostatic stabiliser
B	PHE46	electrostatic stabiliser
B	GLY125	electrostatic stabiliser

site_id	MCSA2
Number of Residues	4
Details	M-CSA 678

Chain	Residue	Details
A	THR2	proton acceptor, proton donor
A	VAL34	electrostatic stabiliser
A	PHE46	electrostatic stabiliser
A	GLY125	electrostatic stabiliser

site_id	MCSA3
Number of Residues	4
Details	M-CSA 678

Chain	Residue	Details
D	THR2	proton acceptor, proton donor
D	VAL34	electrostatic stabiliser
D	PHE46	electrostatic stabiliser
D	GLY125	electrostatic stabiliser

site_id	MCSA4
Number of Residues	4
Details	M-CSA 678

Chain	Residue	Details
C	THR2	proton acceptor, proton donor
C	VAL34	electrostatic stabiliser
C	PHE46	electrostatic stabiliser
C	GLY125	electrostatic stabiliser

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