1IXS
Structure of RuvB complexed with RuvA domain III
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006281 | biological_process | DNA repair |
A | 0006310 | biological_process | DNA recombination |
A | 0009378 | molecular_function | four-way junction helicase activity |
A | 0009379 | cellular_component | Holliday junction helicase complex |
B | 0000400 | molecular_function | four-way junction DNA binding |
B | 0003677 | molecular_function | DNA binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006281 | biological_process | DNA repair |
B | 0006310 | biological_process | DNA recombination |
B | 0009378 | molecular_function | four-way junction helicase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0032508 | biological_process | DNA duplex unwinding |
B | 0048476 | cellular_component | Holliday junction resolvase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ANP B 319 |
Chain | Residue |
B | ARG7 |
B | ARG205 |
B | LYS208 |
B | TYR14 |
B | ILE15 |
B | GLY50 |
B | LYS51 |
B | THR52 |
B | THR53 |
B | TYR168 |
B | MET204 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11171970, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1HQC, ECO:0000312|PDB:1IXS |
Chain | Residue | Details |
B | TYR14 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11171970, ECO:0000312|PDB:1HQC, ECO:0000312|PDB:1IXS |
Chain | Residue | Details |
B | ILE15 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1IXR |
Chain | Residue | Details |
B | GLY48 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1IXR, ECO:0000312|PDB:1IXS |
Chain | Residue | Details |
B | LYS51 | |
B | THR53 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016 |
Chain | Residue | Details |
B | THR52 | |
B | ARG297 | |
B | ARG302 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:12408833 |
Chain | Residue | Details |
B | ASP97 | |
B | THR146 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000269|PubMed:11171970, ECO:0000269|PubMed:12408833, ECO:0000312|PDB:1HQC, ECO:0000312|PDB:1IXS |
Chain | Residue | Details |
B | TYR168 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00016, ECO:0000305|PubMed:12408833 |
Chain | Residue | Details |
B | ARG205 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 780 |
Chain | Residue | Details |
B | LYS51 | |
B | THR52 | |
B | ASP97 | |
B | THR146 | electrostatic stabiliser |
B | ARG205 | electrostatic stabiliser |