1OFI
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 | 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 | 0030163 | biological_process | protein catabolic process |
G | 0046872 | molecular_function | metal ion binding |
G | 0051603 | biological_process | proteolysis involved in protein catabolic process |
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 | 0030163 | biological_process | protein catabolic process |
H | 0046872 | molecular_function | metal ion binding |
H | 0051603 | biological_process | proteolysis involved in protein catabolic process |
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 | 0030163 | biological_process | protein catabolic process |
I | 0046872 | molecular_function | metal ion binding |
I | 0051603 | biological_process | proteolysis involved in protein catabolic process |
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 | 0030163 | biological_process | protein catabolic process |
L | 0046872 | molecular_function | metal ion binding |
L | 0051603 | biological_process | proteolysis involved in protein catabolic process |
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 | 0030163 | biological_process | protein catabolic process |
M | 0046872 | molecular_function | metal ion binding |
M | 0051603 | biological_process | proteolysis involved in protein catabolic process |
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 | 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 | HOH2003 |
A | HOH2005 |
A | HOH2007 |
A | THR59 |
A | LYS63 |
A | GLU258 |
A | GLU322 |
A | ADP450 |
A | MG451 |
A | MG453 |
A | HOH2002 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 B 452 |
Chain | Residue |
B | PRO58 |
B | THR59 |
B | GLY60 |
B | LYS63 |
B | GLU258 |
B | ADP450 |
B | MG451 |
B | MG453 |
B | HOH2004 |
C | GLU322 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PO4 C 452 |
Chain | Residue |
B | GLU322 |
C | PRO58 |
C | THR59 |
C | GLY60 |
C | GLU258 |
C | ADP450 |
C | MG451 |
C | MG453 |
C | HOH2002 |
C | HOH2006 |
C | HOH2007 |
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 | 4 |
Details | BINDING SITE FOR RESIDUE MG L 454 |
Chain | Residue |
L | GLY157 |
L | CYS160 |
L | VAL161 |
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 | HOH2001 |
A | HOH2002 |
A | HOH2006 |
A | HOH2007 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 453 |
Chain | Residue |
A | GLU258 |
A | GLU322 |
A | PO4452 |
A | HOH2003 |
A | HOH2004 |
A | HOH2005 |
A | HOH2007 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 451 |
Chain | Residue |
B | ADP450 |
B | PO4452 |
B | HOH2001 |
B | HOH2004 |
B | HOH2005 |
B | HOH2006 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 453 |
Chain | Residue |
B | GLU258 |
B | PO4452 |
B | HOH2002 |
B | HOH2007 |
C | GLU322 |
C | HOH2004 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 451 |
Chain | Residue |
C | ADP450 |
C | PO4452 |
C | HOH2001 |
C | HOH2002 |
C | HOH2005 |
C | HOH2007 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 453 |
Chain | Residue |
B | GLU322 |
B | HOH2003 |
C | GLU258 |
C | PO4452 |
C | HOH2003 |
C | HOH2006 |
site_id | BC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP A 450 |
Chain | Residue |
A | GLU65 |
A | GLU287 |
A | LEU336 |
A | ALA393 |
A | MG451 |
A | PO4452 |
A | HOH2001 |
A | HOH2006 |
A | HIS16 |
A | ILE17 |
A | ILE18 |
A | PRO58 |
A | THR59 |
A | GLY60 |
A | VAL61 |
A | GLY62 |
A | LYS63 |
A | THR64 |
site_id | BC8 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP B 450 |
Chain | Residue |
B | HIS16 |
B | ILE17 |
B | ILE18 |
B | GLN20 |
B | PRO58 |
B | GLY60 |
B | VAL61 |
B | GLY62 |
B | LYS63 |
B | THR64 |
B | GLU65 |
B | LEU336 |
B | ALA393 |
B | MG451 |
B | PO4452 |
B | HOH2004 |
B | HOH2005 |
B | HOH2006 |
site_id | BC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADP C 450 |
Chain | Residue |
C | HIS16 |
C | ILE17 |
C | ILE18 |
C | PRO58 |
C | THR59 |
C | GLY60 |
C | VAL61 |
C | GLY62 |
C | LYS63 |
C | THR64 |
C | GLU65 |
C | ALA393 |
C | MG451 |
C | PO4452 |
C | HOH2005 |
site_id | CC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE LVS G 0 |
Chain | Residue |
G | THR1 |
G | GLN19 |
G | VAL20 |
G | SER21 |
G | MET27 |
G | LYS33 |
G | PHE46 |
G | ALA47 |
G | GLY48 |
G | THR50 |
G | THR107 |
G | ILE109 |
G | ASP111 |
G | GLY124 |
G | SER125 |
site_id | CC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE LVS H 0 |
Chain | Residue |
H | THR1 |
H | VAL20 |
H | SER21 |
H | LYS33 |
H | PHE46 |
H | ALA47 |
H | GLY48 |
H | THR50 |
H | GLY124 |
H | SER125 |
I | THR107 |
site_id | CC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE LVS I 0 |
Chain | Residue |
H | GLU92 |
I | THR1 |
I | VAL20 |
I | SER21 |
I | PHE46 |
I | GLY48 |
I | THR50 |
I | GLY124 |
I | SER125 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: |
Chain | Residue | Details |
G | THR2 | |
H | THR2 | |
I | THR2 | |
L | THR2 | |
M | THR2 | |
N | THR2 | |
C | ILE18 | |
C | GLY60 | |
C | ILE306 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: |
Chain | Residue | Details |
G | ASP158 | |
L | ASP158 | |
L | VAL161 | |
L | ASN164 | |
M | ASP158 | |
M | VAL161 | |
M | ASN164 | |
N | ASP158 | |
N | VAL161 | |
N | ASN164 | |
G | VAL161 | |
G | ASN164 | |
H | ASP158 | |
H | VAL161 | |
H | ASN164 | |
I | ASP158 | |
I | VAL161 | |
I | ASN164 |
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 |