1M4Y
Crystal structure of HslV from Thermotoga maritima
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000502 | cellular_component | proteasome complex |
A | 0004298 | molecular_function | threonine-type endopeptidase activity |
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 | 0000502 | cellular_component | proteasome complex |
B | 0004298 | molecular_function | threonine-type endopeptidase activity |
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 | 0000502 | cellular_component | proteasome complex |
C | 0004298 | molecular_function | threonine-type endopeptidase activity |
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 | 6 |
Details | BINDING SITE FOR RESIDUE NA C 250 |
Chain | Residue |
C | GLY156 |
C | CYS159 |
C | THR162 |
C | HOH268 |
C | HOH288 |
C | HOH301 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 251 |
Chain | Residue |
B | HOH253 |
B | HOH271 |
B | HOH290 |
B | GLY156 |
B | CYS159 |
B | THR162 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 252 |
Chain | Residue |
A | GLY156 |
A | CYS159 |
A | THR162 |
A | HOH257 |
A | HOH273 |
A | HOH294 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | THR1 | |
B | THR1 | |
C | THR1 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12646382 |
Chain | Residue | Details |
A | GLY156 | |
A | CYS159 | |
A | THR162 | |
B | GLY156 | |
B | CYS159 | |
B | THR162 | |
C | GLY156 | |
C | CYS159 | |
C | THR162 |
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 | SER124 |
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 | SER124 |
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 | SER124 |
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 | 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 |
C | GLY45 | |
C | LYS33 | |
C | THR1 | |
C | SER124 |