1HQC
STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000400 | molecular_function | four-way junction DNA binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006281 | biological_process | DNA repair |
| A | 0006310 | biological_process | DNA recombination |
| A | 0006974 | biological_process | DNA damage response |
| A | 0009378 | molecular_function | four-way junction helicase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0048476 | cellular_component | Holliday junction resolvase complex |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0006974 | biological_process | DNA damage response |
| B | 0009378 | molecular_function | four-way junction helicase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0048476 | cellular_component | Holliday junction resolvase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | THR52 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 402 |
| Chain | Residue |
| B | VAL68 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ADE A 501 |
| Chain | Residue |
| A | TYR14 |
| A | ILE15 |
| A | THR53 |
| A | ARG179 |
| A | LYS208 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ADE B 502 |
| Chain | Residue |
| B | ILE15 |
| B | TYR168 |
| B | LYS208 |
| B | ARG7 |
| B | TYR14 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 140 |
| Details | Region: {"description":"Small ATPAse domain (RuvB-S)","evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11171970","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11171970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HQC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1IXS","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11171970","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HQC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1IXS","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IXR","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IXR","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1IXS","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11171970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HQC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1IXS","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00016","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12408833","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 10464259, 11171970 |
| Chain | Residue | Details |
| A | THR146 | |
| A | ARG205 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 10464259, 11171970 |
| Chain | Residue | Details |
| B | THR146 | |
| B | ARG205 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 780 |
| Chain | Residue | Details |
| A | LYS51 | |
| A | THR52 | |
| A | ASP97 | |
| A | THR146 | electrostatic stabiliser |
| A | ARG205 | electrostatic stabiliser |
| site_id | MCSA2 |
| 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 |
