6P8J
Structure of P. aeruginosa ATCC27853 CdnD D62N/D64N mutant bound to ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051607 | biological_process | defense response to virus |
| A | 0106408 | molecular_function | diadenylate cyclase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051607 | biological_process | defense response to virus |
| B | 0106408 | molecular_function | diadenylate cyclase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0009117 | biological_process | nucleotide metabolic process |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051607 | biological_process | defense response to virus |
| C | 0106408 | molecular_function | diadenylate cyclase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0009117 | biological_process | nucleotide metabolic process |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051607 | biological_process | defense response to virus |
| D | 0106408 | molecular_function | diadenylate cyclase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | binding site for residue ATP C 401 |
| Chain | Residue |
| C | GLY49 |
| C | HIS159 |
| C | LYS182 |
| C | SER199 |
| C | PHE200 |
| C | ASP239 |
| C | GLY244 |
| C | PRO245 |
| C | ILE247 |
| C | MG403 |
| C | HOH521 |
| C | SER50 |
| C | HOH537 |
| C | HOH588 |
| C | HOH605 |
| C | HOH635 |
| C | HOH643 |
| C | HOH679 |
| C | HOH684 |
| C | ARG53 |
| C | LYS56 |
| C | ASN62 |
| C | ASN64 |
| C | ARG106 |
| C | ASP130 |
| C | THR154 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 402 |
| Chain | Residue |
| C | LYS194 |
| C | ARG255 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 403 |
| Chain | Residue |
| C | ASN62 |
| C | ASN64 |
| C | ASP130 |
| C | ATP401 |
| C | HOH684 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | binding site for residue ATP A 401 |
| Chain | Residue |
| A | GLY49 |
| A | SER50 |
| A | ARG53 |
| A | LYS56 |
| A | ASN62 |
| A | ASN64 |
| A | ARG106 |
| A | ASP130 |
| A | THR154 |
| A | HIS159 |
| A | LYS182 |
| A | SER199 |
| A | PHE200 |
| A | ASP239 |
| A | GLY244 |
| A | PRO245 |
| A | ILE247 |
| A | MG403 |
| A | HOH547 |
| A | HOH574 |
| A | HOH580 |
| A | HOH594 |
| A | HOH653 |
| A | HOH712 |
| A | HOH726 |
| A | HOH729 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | LYS194 |
| A | ARG255 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASN62 |
| A | ASN64 |
| A | ASP130 |
| A | ATP401 |
| A | HOH653 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | binding site for residue ATP B 401 |
| Chain | Residue |
| B | GLY49 |
| B | SER50 |
| B | ARG53 |
| B | LYS56 |
| B | ASN62 |
| B | ASN64 |
| B | ARG106 |
| B | ASP130 |
| B | LYS153 |
| B | THR154 |
| B | HIS159 |
| B | LYS182 |
| B | SER199 |
| B | PHE200 |
| B | ASP239 |
| B | GLY244 |
| B | PRO245 |
| B | ILE247 |
| B | MG403 |
| B | HOH523 |
| B | HOH559 |
| B | HOH596 |
| B | HOH600 |
| B | HOH619 |
| B | HOH634 |
| B | HOH650 |
| B | HOH682 |
| B | HOH687 |
| B | HOH705 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 402 |
| Chain | Residue |
| B | LYS194 |
| B | ARG255 |
| B | HOH838 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | ASN64 |
| B | ASP130 |
| B | ATP401 |
| B | HOH619 |
| B | ASN62 |
| site_id | AD1 |
| Number of Residues | 27 |
| Details | binding site for residue ATP D 401 |
| Chain | Residue |
| D | GLY49 |
| D | SER50 |
| D | ARG53 |
| D | LYS56 |
| D | ASN62 |
| D | ASN64 |
| D | ASP130 |
| D | THR154 |
| D | HIS159 |
| D | LYS182 |
| D | SER199 |
| D | PHE200 |
| D | ASP239 |
| D | GLY244 |
| D | PRO245 |
| D | ILE247 |
| D | MG403 |
| D | HOH532 |
| D | HOH562 |
| D | HOH592 |
| D | HOH607 |
| D | HOH608 |
| D | HOH614 |
| D | HOH656 |
| D | HOH665 |
| D | HOH669 |
| D | HOH716 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 402 |
| Chain | Residue |
| D | LYS194 |
| D | ARG255 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 403 |
| Chain | Residue |
| D | ASN62 |
| D | ASN64 |
| D | ASP130 |
| D | ATP401 |
| D | HOH665 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31932165, ECO:0007744|PDB:6P8J |
| Chain | Residue | Details |
| C | SER50 | |
| C | PRO245 | |
| A | SER50 | |
| A | ARG53 | |
| A | LYS56 | |
| A | ASN62 | |
| A | ASN64 | |
| A | ASP130 | |
| A | THR154 | |
| A | LYS182 | |
| A | SER199 | |
| C | ARG53 | |
| A | PRO245 | |
| B | SER50 | |
| B | ARG53 | |
| B | LYS56 | |
| B | ASN62 | |
| B | ASN64 | |
| B | ASP130 | |
| B | THR154 | |
| B | LYS182 | |
| B | SER199 | |
| C | LYS56 | |
| B | PRO245 | |
| D | SER50 | |
| D | ARG53 | |
| D | LYS56 | |
| D | ASN62 | |
| D | ASN64 | |
| D | ASP130 | |
| D | THR154 | |
| D | LYS182 | |
| D | SER199 | |
| C | ASN62 | |
| D | PRO245 | |
| C | ASN64 | |
| C | ASP130 | |
| C | THR154 | |
| C | LYS182 | |
| C | SER199 |
