4U7D
Structure of human RECQ-like helicase in complex with an oligonucleotide
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 |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004386 | molecular_function | helicase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006310 | biological_process | DNA recombination |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0004386 | molecular_function | helicase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006310 | biological_process | DNA recombination |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 701 |
| Chain | Residue |
| A | CYS453 |
| A | CYS471 |
| A | CYS475 |
| A | CYS478 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 701 |
| Chain | Residue |
| B | CYS453 |
| B | CYS471 |
| B | CYS475 |
| B | CYS478 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 701 |
| Chain | Residue |
| C | CYS471 |
| C | CYS475 |
| C | CYS478 |
| C | CYS453 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 701 |
| Chain | Residue |
| D | CYS453 |
| D | CYS471 |
| D | CYS475 |
| D | CYS478 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:19151156 |
| Chain | Residue | Details |
| A | LYS119 | |
| B | LYS119 | |
| C | LYS119 | |
| D | LYS119 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19151156, ECO:0007744|PDB:2V1X |
| Chain | Residue | Details |
| A | LYS91 | |
| B | GLN96 | |
| B | GLY116 | |
| B | GLY118 | |
| B | LYS119 | |
| B | SER120 | |
| C | LYS91 | |
| C | ARG93 | |
| C | GLN96 | |
| C | GLY116 | |
| C | GLY118 | |
| A | ARG93 | |
| C | LYS119 | |
| C | SER120 | |
| D | LYS91 | |
| D | ARG93 | |
| D | GLN96 | |
| D | GLY116 | |
| D | GLY118 | |
| D | LYS119 | |
| D | SER120 | |
| A | GLN96 | |
| A | GLY116 | |
| A | GLY118 | |
| A | LYS119 | |
| A | SER120 | |
| B | LYS91 | |
| B | ARG93 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19151156, ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X, ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D |
| Chain | Residue | Details |
| A | CYS453 | |
| C | CYS471 | |
| C | CYS475 | |
| C | CYS478 | |
| D | CYS453 | |
| D | CYS471 | |
| D | CYS475 | |
| D | CYS478 | |
| A | CYS471 | |
| A | CYS475 | |
| A | CYS478 | |
| B | CYS453 | |
| B | CYS471 | |
| B | CYS475 | |
| B | CYS478 | |
| C | CYS453 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS514 | |
| A | LYS522 | |
| B | LYS514 | |
| B | LYS522 | |
| C | LYS514 | |
| C | LYS522 | |
| D | LYS514 | |
| D | LYS522 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER597 | |
| B | SER597 | |
| C | SER597 | |
| D | SER597 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6AYJ1 |
| Chain | Residue | Details |
| A | SER602 | |
| B | SER602 | |
| C | SER602 | |
| D | SER602 |
