2V1X
Crystal structure of human RECQ-like DNA helicase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004386 | molecular_function | helicase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006310 | biological_process | DNA recombination |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004386 | molecular_function | helicase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006310 | biological_process | DNA recombination |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1594 |
| Chain | Residue |
| A | SER120 |
| A | ADP1593 |
| A | HOH2018 |
| A | HOH2033 |
| A | HOH2034 |
| A | HOH2144 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1595 |
| Chain | Residue |
| A | CYS478 |
| A | CYS453 |
| A | CYS471 |
| A | CYS475 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1596 |
| Chain | Residue |
| A | HIS357 |
| A | ASP379 |
| A | LYS380 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 1597 |
| Chain | Residue |
| A | GLU485 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1598 |
| Chain | Residue |
| A | THR115 |
| A | TYR399 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1599 |
| Chain | Residue |
| A | ARG486 |
| A | GLN589 |
| A | HOH2037 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1594 |
| Chain | Residue |
| B | ADP1593 |
| B | HOH2027 |
| B | HOH2037 |
| B | HOH2038 |
| B | HOH2162 |
| B | HOH2165 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1595 |
| Chain | Residue |
| B | CYS453 |
| B | CYS471 |
| B | CYS475 |
| B | CYS478 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 1596 |
| Chain | Residue |
| B | GLN324 |
| B | ALA346 |
| B | THR371 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 1597 |
| Chain | Residue |
| B | GLN324 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1598 |
| Chain | Residue |
| B | HIS357 |
| B | ILE378 |
| B | ASP379 |
| B | LYS380 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 1599 |
| Chain | Residue |
| B | THR115 |
| B | TYR399 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 1600 |
| Chain | Residue |
| B | GLN589 |
| site_id | BC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP A 1593 |
| Chain | Residue |
| A | LEU89 |
| A | LYS91 |
| A | ARG93 |
| A | GLN96 |
| A | PRO114 |
| A | THR115 |
| A | GLY116 |
| A | GLY117 |
| A | GLY118 |
| A | LYS119 |
| A | SER120 |
| A | ASP379 |
| A | MG1594 |
| A | HOH2011 |
| A | HOH2018 |
| A | HOH2033 |
| A | HOH2144 |
| A | HOH2145 |
| A | HOH2146 |
| site_id | BC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP B 1593 |
| Chain | Residue |
| B | LEU89 |
| B | LYS91 |
| B | ARG93 |
| B | GLN96 |
| B | THR115 |
| B | GLY116 |
| B | GLY117 |
| B | GLY118 |
| B | LYS119 |
| B | SER120 |
| B | ASP379 |
| B | MG1594 |
| B | HOH2027 |
| B | HOH2160 |
| B | HOH2161 |
| B | HOH2162 |
| B | HOH2163 |
| B | HOH2164 |
| B | HOH2165 |
| B | HOH2166 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1601 |
| Chain | Residue |
| B | GLN292 |
| B | TYR418 |
| B | PHE420 |
| B | GLU540 |
| B | GLU543 |
| B | HOH2167 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1602 |
| Chain | Residue |
| B | PHE424 |
| B | SER428 |
| B | ILE567 |
| B | SER568 |
| B | HOH2169 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 350 |
| Details | Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 302 |
| Details | Domain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 222 |
| Details | Region: {"description":"Winged-helix domain","evidences":[{"source":"PubMed","id":"19151156","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Motif: {"description":"DEVH box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"19151156","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19151156","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2V1X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19151156","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25831490","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V1X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WWY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4U7D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
