8XVC
CryoEM structure of ADP-DNA-MuB conformation1
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 342 |
| Details | DNA_BIND: H-T-H motif => ECO:0000255 |
| Chain | Residue | Details |
| A | PHE21-ASN40 | |
| J | PHE21-ASN40 | |
| K | PHE21-ASN40 | |
| L | PHE21-ASN40 | |
| M | PHE21-ASN40 | |
| N | PHE21-ASN40 | |
| O | PHE21-ASN40 | |
| P | PHE21-ASN40 | |
| Q | PHE21-ASN40 | |
| R | PHE21-ASN40 | |
| B | PHE21-ASN40 | |
| C | PHE21-ASN40 | |
| D | PHE21-ASN40 | |
| E | PHE21-ASN40 | |
| F | PHE21-ASN40 | |
| G | PHE21-ASN40 | |
| H | PHE21-ASN40 | |
| I | PHE21-ASN40 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1602 |
| Details | DNA_BIND: |
| Chain | Residue | Details |
| A | SER223-ASN312 | |
| J | SER223-ASN312 | |
| K | SER223-ASN312 | |
| L | SER223-ASN312 | |
| M | SER223-ASN312 | |
| N | SER223-ASN312 | |
| O | SER223-ASN312 | |
| P | SER223-ASN312 | |
| Q | SER223-ASN312 | |
| R | SER223-ASN312 | |
| B | SER223-ASN312 | |
| C | SER223-ASN312 | |
| D | SER223-ASN312 | |
| E | SER223-ASN312 | |
| F | SER223-ASN312 | |
| G | SER223-ASN312 | |
| H | SER223-ASN312 | |
| I | SER223-ASN312 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY100 | |
| J | GLY100 | |
| K | GLY100 | |
| L | GLY100 | |
| M | GLY100 | |
| N | GLY100 | |
| O | GLY100 | |
| P | GLY100 | |
| Q | GLY100 | |
| R | GLY100 | |
| B | GLY100 | |
| C | GLY100 | |
| D | GLY100 | |
| E | GLY100 | |
| F | GLY100 | |
| G | GLY100 | |
| H | GLY100 | |
| I | GLY100 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | SITE: Involved in DNA binding => ECO:0000269|PubMed:23776210 |
| Chain | Residue | Details |
| A | ARG151 | |
| E | LYS152 | |
| F | ARG151 | |
| F | LYS152 | |
| G | ARG151 | |
| G | LYS152 | |
| H | ARG151 | |
| H | LYS152 | |
| I | ARG151 | |
| I | LYS152 | |
| J | ARG151 | |
| A | LYS152 | |
| J | LYS152 | |
| K | ARG151 | |
| K | LYS152 | |
| L | ARG151 | |
| L | LYS152 | |
| M | ARG151 | |
| M | LYS152 | |
| N | ARG151 | |
| N | LYS152 | |
| O | ARG151 | |
| B | ARG151 | |
| O | LYS152 | |
| P | ARG151 | |
| P | LYS152 | |
| Q | ARG151 | |
| Q | LYS152 | |
| R | ARG151 | |
| R | LYS152 | |
| B | LYS152 | |
| C | ARG151 | |
| C | LYS152 | |
| D | ARG151 | |
| D | LYS152 | |
| E | ARG151 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | SITE: Sensor-1; involved in ATP-binding and hydrolysis => ECO:0000269|PubMed:23776210 |
| Chain | Residue | Details |
| A | ASN202 | |
| J | ASN202 | |
| K | ASN202 | |
| L | ASN202 | |
| M | ASN202 | |
| N | ASN202 | |
| O | ASN202 | |
| P | ASN202 | |
| Q | ASN202 | |
| R | ASN202 | |
| B | ASN202 | |
| C | ASN202 | |
| D | ASN202 | |
| E | ASN202 | |
| F | ASN202 | |
| G | ASN202 | |
| H | ASN202 | |
| I | ASN202 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 18 |
| Details | SITE: R-finger; involved in ATP-binding => ECO:0000269|PubMed:23776210 |
| Chain | Residue | Details |
| A | ARG224 | |
| J | ARG224 | |
| K | ARG224 | |
| L | ARG224 | |
| M | ARG224 | |
| N | ARG224 | |
| O | ARG224 | |
| P | ARG224 | |
| Q | ARG224 | |
| R | ARG224 | |
| B | ARG224 | |
| C | ARG224 | |
| D | ARG224 | |
| E | ARG224 | |
| F | ARG224 | |
| G | ARG224 | |
| H | ARG224 | |
| I | ARG224 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 18 |
| Details | SITE: Sensor-2; involved in ATP-binding and hydrolysis => ECO:0000269|PubMed:23776210 |
| Chain | Residue | Details |
| A | ARG268 | |
| J | ARG268 | |
| K | ARG268 | |
| L | ARG268 | |
| M | ARG268 | |
| N | ARG268 | |
| O | ARG268 | |
| P | ARG268 | |
| Q | ARG268 | |
| R | ARG268 | |
| B | ARG268 | |
| C | ARG268 | |
| D | ARG268 | |
| E | ARG268 | |
| F | ARG268 | |
| G | ARG268 | |
| H | ARG268 | |
| I | ARG268 |
