1JJW
Structure of Haemophilus influenzae HslV Protein at 1.9 A Resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004298 | molecular_function | threonine-type endopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
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 | 0030163 | biological_process | protein catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051603 | biological_process | proteolysis involved in protein catabolic process |
B | 0004298 | molecular_function | threonine-type endopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
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 | 0030163 | biological_process | protein catabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051603 | biological_process | proteolysis involved in protein catabolic process |
C | 0004298 | molecular_function | threonine-type endopeptidase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
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 | 0030163 | biological_process | protein catabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0051603 | biological_process | proteolysis involved in protein catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K A 501 |
Chain | Residue |
A | GLY157 |
A | CYS160 |
A | THR163 |
A | HOH236 |
A | HOH237 |
A | HOH238 |
B | HOH346 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K B 502 |
Chain | Residue |
B | CYS160 |
B | THR163 |
B | HOH334 |
B | HOH336 |
A | HOH335 |
B | GLY157 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K C 503 |
Chain | Residue |
C | GLY157 |
C | CYS160 |
C | THR163 |
C | HOH438 |
C | HOH439 |
C | HOH454 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | THR2 | |
B | THR2 | |
C | THR2 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP158 | |
A | VAL161 | |
A | ASN164 | |
B | ASP158 | |
B | VAL161 | |
B | ASN164 | |
C | ASP158 | |
C | VAL161 | |
C | ASN164 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1pma |
Chain | Residue | Details |
A | GLY48 | |
A | LYS33 | |
A | THR1 | |
A | SER125 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1pma |
Chain | Residue | Details |
B | GLY48 | |
B | LYS33 | |
B | THR1 | |
B | SER125 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1pma |
Chain | Residue | Details |
C | GLY48 | |
C | LYS33 | |
C | THR1 | |
C | SER125 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1pma |
Chain | Residue | Details |
A | GLY45 | |
A | LYS33 | |
A | THR1 | |
A | SER125 |
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 | SER125 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1pma |
Chain | Residue | Details |
C | GLY45 | |
C | LYS33 | |
C | THR1 | |
C | SER125 |