Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OFH

Asymmetric complex between HslV and I-domain deleted HslU (H. influenzae)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0008233	molecular_function	peptidase activity
A	0009376	cellular_component	HslUV protease complex
A	0016887	molecular_function	ATP hydrolysis activity
B	0005524	molecular_function	ATP binding
B	0008233	molecular_function	peptidase activity
B	0009376	cellular_component	HslUV protease complex
B	0016887	molecular_function	ATP hydrolysis activity
C	0005524	molecular_function	ATP binding
C	0008233	molecular_function	peptidase activity
C	0009376	cellular_component	HslUV protease complex
C	0016887	molecular_function	ATP hydrolysis activity
G	0003824	molecular_function	catalytic activity
G	0004298	molecular_function	threonine-type endopeptidase activity
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005839	cellular_component	proteasome core complex
G	0006508	biological_process	proteolysis
G	0008233	molecular_function	peptidase activity
G	0009376	cellular_component	HslUV protease complex
G	0016787	molecular_function	hydrolase activity
G	0030163	biological_process	protein catabolic process
G	0046872	molecular_function	metal ion binding
G	0051603	biological_process	proteolysis involved in protein catabolic process
H	0003824	molecular_function	catalytic activity
H	0004298	molecular_function	threonine-type endopeptidase activity
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005839	cellular_component	proteasome core complex
H	0006508	biological_process	proteolysis
H	0008233	molecular_function	peptidase activity
H	0009376	cellular_component	HslUV protease complex
H	0016787	molecular_function	hydrolase activity
H	0030163	biological_process	protein catabolic process
H	0046872	molecular_function	metal ion binding
H	0051603	biological_process	proteolysis involved in protein catabolic process
I	0003824	molecular_function	catalytic activity
I	0004298	molecular_function	threonine-type endopeptidase activity
I	0005515	molecular_function	protein binding
I	0005737	cellular_component	cytoplasm
I	0005839	cellular_component	proteasome core complex
I	0006508	biological_process	proteolysis
I	0008233	molecular_function	peptidase activity
I	0009376	cellular_component	HslUV protease complex
I	0016787	molecular_function	hydrolase activity
I	0030163	biological_process	protein catabolic process
I	0046872	molecular_function	metal ion binding
I	0051603	biological_process	proteolysis involved in protein catabolic process
L	0003824	molecular_function	catalytic activity
L	0004298	molecular_function	threonine-type endopeptidase activity
L	0005515	molecular_function	protein binding
L	0005737	cellular_component	cytoplasm
L	0005839	cellular_component	proteasome core complex
L	0006508	biological_process	proteolysis
L	0008233	molecular_function	peptidase activity
L	0009376	cellular_component	HslUV protease complex
L	0016787	molecular_function	hydrolase activity
L	0030163	biological_process	protein catabolic process
L	0046872	molecular_function	metal ion binding
L	0051603	biological_process	proteolysis involved in protein catabolic process
M	0003824	molecular_function	catalytic activity
M	0004298	molecular_function	threonine-type endopeptidase activity
M	0005515	molecular_function	protein binding
M	0005737	cellular_component	cytoplasm
M	0005839	cellular_component	proteasome core complex
M	0006508	biological_process	proteolysis
M	0008233	molecular_function	peptidase activity
M	0009376	cellular_component	HslUV protease complex
M	0016787	molecular_function	hydrolase activity
M	0030163	biological_process	protein catabolic process
M	0046872	molecular_function	metal ion binding
M	0051603	biological_process	proteolysis involved in protein catabolic process
N	0003824	molecular_function	catalytic activity
N	0004298	molecular_function	threonine-type endopeptidase activity
N	0005515	molecular_function	protein binding
N	0005737	cellular_component	cytoplasm
N	0005839	cellular_component	proteasome core complex
N	0006508	biological_process	proteolysis
N	0008233	molecular_function	peptidase activity
N	0009376	cellular_component	HslUV protease complex
N	0016787	molecular_function	hydrolase activity
N	0030163	biological_process	protein catabolic process
N	0046872	molecular_function	metal ion binding
N	0051603	biological_process	proteolysis involved in protein catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 A 452

Chain	Residue
A	PRO58
A	HOH2006
A	HOH2010
A	HOH2020
A	THR59
A	LYS63
A	GLU258
A	GLU322
A	ADP450
A	MG451
A	MG453
A	HOH2005

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PO4 B 452

Chain	Residue
B	GLY57
B	PRO58
B	THR59
B	LYS63
B	ASP257
B	GLU258
B	ADP450
B	MG451
B	MG453
B	HOH2009
B	HOH2011
B	HOH2027
C	GLU322

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PO4 C 452

Chain	Residue
B	GLU322
B	HOH2019
C	PRO58
C	THR59
C	GLY60
C	LYS63
C	GLU258
C	ADP450
C	MG451
C	MG453
C	HOH2011
C	HOH2031

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG G 454

Chain	Residue
G	GLY157
G	CYS160
G	THR163

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG H 454

Chain	Residue
H	GLY157
H	CYS160
H	THR163

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG I 454

Chain	Residue
I	GLY157
I	CYS160
I	THR163

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG L 454

Chain	Residue
L	GLY157
L	CYS160
L	THR163

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG M 454

Chain	Residue
M	GLY157
M	CYS160
M	THR163

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG N 454

Chain	Residue
N	GLY157
N	CYS160
N	THR163

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 451

Chain	Residue
A	ADP450
A	PO4452
A	HOH2005
A	HOH2006
A	HOH2019
A	HOH2020

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 453

Chain	Residue
A	GLU258
A	GLU322
A	PO4452
A	HOH2007
A	HOH2008
A	HOH2010

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 451

Chain	Residue
B	ADP450
B	PO4452
B	HOH2011
B	HOH2012
B	HOH2027
B	HOH2028

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 453

Chain	Residue
B	GLU258
B	PO4452
B	HOH2009
B	HOH2013
C	GLU322
C	HOH2013

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 451

Chain	Residue
B	HOH2019
C	ADP450
C	PO4452
C	HOH2028
C	HOH2029
C	HOH2031

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 453

Chain	Residue
B	GLU322
B	HOH2014
B	HOH2020
C	GLU258
C	PO4452
C	HOH2012

site_id	BC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ADP A 450

Chain	Residue
A	GLU65
A	ALA393
A	MG451
A	PO4452
A	HOH2006
A	HOH2019
A	HOH2020
A	HIS16
A	ILE18
A	PRO58
A	GLY60
A	VAL61
A	GLY62
A	LYS63
A	THR64

site_id	BC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP B 450

Chain	Residue
B	HIS16
B	ILE17
B	ILE18
B	PRO58
B	GLY60
B	VAL61
B	GLY62
B	LYS63
B	THR64
B	GLU65
B	ALA393
B	MG451
B	PO4452
B	HOH2011
B	HOH2027
B	HOH2028

site_id	BC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ADP C 450

Chain	Residue
B	HOH2019
C	HIS16
C	ILE17
C	ILE18
C	PRO58
C	GLY60
C	VAL61
C	GLY62
C	LYS63
C	THR64
C	GLU65
C	LEU336
C	ILE344
C	ALA393
C	MG451
C	PO4452
C	HOH2008
C	HOH2028
C	HOH2029

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	27
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11106733","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Active site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
G	GLY48
G	LYS33
G	THR1
G	SER125

site_id	CSA10
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
L	GLY45
L	LYS33
L	THR1
L	SER125

site_id	CSA11
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
M	GLY45
M	LYS33
M	THR1
M	SER125

site_id	CSA12
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
N	GLY45
N	LYS33
N	THR1
N	SER125

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

Chain	Residue	Details
H	GLY48
H	LYS33
H	THR1
H	SER125

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

Chain	Residue	Details
I	GLY48
I	LYS33
I	THR1
I	SER125

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

Chain	Residue	Details
L	GLY48
L	LYS33
L	THR1
L	SER125

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

Chain	Residue	Details
M	GLY48
M	LYS33
M	THR1
M	SER125

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

Chain	Residue	Details
N	GLY48
N	LYS33
N	THR1
N	SER125

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

Chain	Residue	Details
G	GLY45
G	LYS33
G	THR1
G	SER125

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

Chain	Residue	Details
H	GLY45
H	LYS33
H	THR1
H	SER125

site_id	CSA9
Number of Residues	4
Details	Annotated By Reference To The Literature 1pma

Chain	Residue	Details
I	GLY45
I	LYS33
I	THR1
I	SER125

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