2XXA
The Crystal Structure of the Signal Recognition Particle (SRP) in Complex with its Receptor(SR)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
A | 0003924 | molecular_function | GTPase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006612 | biological_process | protein targeting to membrane |
A | 0006614 | biological_process | SRP-dependent cotranslational protein targeting to membrane |
A | 0008312 | molecular_function | 7S RNA binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0048500 | cellular_component | signal recognition particle |
A | 1990904 | cellular_component | ribonucleoprotein complex |
B | 0005525 | molecular_function | GTP binding |
B | 0006614 | biological_process | SRP-dependent cotranslational protein targeting to membrane |
B | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0003723 | molecular_function | RNA binding |
C | 0003924 | molecular_function | GTPase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005525 | molecular_function | GTP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006612 | biological_process | protein targeting to membrane |
C | 0006614 | biological_process | SRP-dependent cotranslational protein targeting to membrane |
C | 0008312 | molecular_function | 7S RNA binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0048500 | cellular_component | signal recognition particle |
C | 1990904 | cellular_component | ribonucleoprotein complex |
D | 0005525 | molecular_function | GTP binding |
D | 0006614 | biological_process | SRP-dependent cotranslational protein targeting to membrane |
D | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE GCP A 600 |
Chain | Residue |
A | GLY110 |
A | GLN147 |
A | GLY193 |
A | THR248 |
A | LYS249 |
A | ASP251 |
A | GLY274 |
A | VAL275 |
A | GLY276 |
A | GLU277 |
A | MG601 |
A | ALA111 |
A | HOH2001 |
A | HOH2002 |
A | HOH2003 |
B | ASN107 |
B | ARG138 |
B | LEU192 |
B | GCP600 |
A | GLY112 |
A | LYS113 |
A | THR114 |
A | THR115 |
A | LYS119 |
A | ASP138 |
A | ARG141 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 601 |
Chain | Residue |
A | THR114 |
A | GCP600 |
A | HOH2001 |
A | HOH2002 |
A | HOH2003 |
site_id | AC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE GCP B 600 |
Chain | Residue |
A | GLN109 |
A | ARG141 |
A | GCP600 |
B | ASN107 |
B | GLY108 |
B | VAL109 |
B | GLY110 |
B | LYS111 |
B | THR112 |
B | THR113 |
B | LYS117 |
B | ASP135 |
B | ARG138 |
B | GLN144 |
B | GLY190 |
B | LYS252 |
B | ASP254 |
B | GLY277 |
B | VAL278 |
B | GLY279 |
B | GLU280 |
B | MG601 |
B | HOH2001 |
B | HOH2002 |
B | HOH2003 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
B | THR112 |
B | ARG138 |
B | GCP600 |
B | HOH2001 |
B | HOH2002 |
B | HOH2003 |
site_id | AC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE GCP C 600 |
Chain | Residue |
C | GLY110 |
C | ALA111 |
C | GLY112 |
C | LYS113 |
C | THR114 |
C | THR115 |
C | LYS119 |
C | ASP138 |
C | ARG141 |
C | GLN147 |
C | GLY193 |
C | THR248 |
C | LYS249 |
C | ASP251 |
C | GLY274 |
C | VAL275 |
C | GLY276 |
C | GLU277 |
C | MG601 |
C | HOH2001 |
C | HOH2002 |
C | HOH2003 |
D | ASN107 |
D | ARG138 |
D | LEU192 |
D | GCP600 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 601 |
Chain | Residue |
C | THR114 |
C | GCP600 |
C | HOH2001 |
C | HOH2002 |
C | HOH2003 |
site_id | AC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE GCP D 600 |
Chain | Residue |
D | VAL109 |
D | GLY110 |
D | LYS111 |
D | THR112 |
D | THR113 |
D | LYS117 |
D | ASP135 |
D | ARG138 |
D | GLN144 |
D | GLY190 |
D | LYS252 |
D | ASP254 |
D | GLY277 |
D | VAL278 |
D | GLY279 |
D | GLU280 |
D | MG601 |
D | HOH2001 |
D | HOH2002 |
D | HOH2003 |
C | GLN109 |
C | ARG141 |
C | LEU195 |
C | GCP600 |
D | ASN107 |
D | GLY108 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 601 |
Chain | Residue |
D | THR112 |
D | ARG138 |
D | GCP600 |
D | HOH2001 |
D | HOH2002 |
D | HOH2003 |
Functional Information from PROSITE/UniProt
site_id | PS00300 |
Number of Residues | 14 |
Details | SRP54 SRP54-type proteins GTP-binding domain signature. PIrYIGVGErIedL |
Chain | Residue | Details |
B | PRO272-LEU285 | |
A | PRO269-LEU282 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00920 |
Chain | Residue | Details |
B | GLY105 | |
B | ASP187 | |
B | THR251 | |
D | GLY105 | |
D | ASP187 | |
D | THR251 |