4H54
Crystal structure of the diguanylate cyclase DgcZ
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043709 | biological_process | cell adhesion involved in single-species biofilm formation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052621 | molecular_function | diguanylate cyclase activity |
| A | 0060187 | cellular_component | cell pole |
| A | 1900233 | biological_process | positive regulation of single-species biofilm formation on inanimate substrate |
| A | 1902201 | biological_process | negative regulation of bacterial-type flagellum-dependent cell motility |
| A | 1902209 | biological_process | negative regulation of bacterial-type flagellum assembly |
| B | 0005515 | molecular_function | protein binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043709 | biological_process | cell adhesion involved in single-species biofilm formation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052621 | molecular_function | diguanylate cyclase activity |
| B | 0060187 | cellular_component | cell pole |
| B | 1900233 | biological_process | positive regulation of single-species biofilm formation on inanimate substrate |
| B | 1902201 | biological_process | negative regulation of bacterial-type flagellum-dependent cell motility |
| B | 1902209 | biological_process | negative regulation of bacterial-type flagellum assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS22 |
| A | HIS79 |
| A | HIS83 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GAV A 402 |
| Chain | Residue |
| A | LYS170 |
| A | ASN173 |
| A | HIS178 |
| A | ASP182 |
| A | LEU185 |
| A | ARG204 |
| A | GLY207 |
| A | GLU208 |
| A | LYS277 |
| A | ARG281 |
| A | MG403 |
| B | ARG140 |
| B | TYR205 |
| A | LEU134 |
| A | ASP165 |
| A | ILE166 |
| A | ASP167 |
| A | ARG168 |
| A | PHE169 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | ASP165 |
| A | ILE166 |
| A | GLU208 |
| A | LYS277 |
| A | GAV402 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GAV A 404 |
| Chain | Residue |
| A | GLU200 |
| A | LYS215 |
| A | ALA225 |
| A | ARG228 |
| A | C2E405 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE C2E A 405 |
| Chain | Residue |
| A | SER194 |
| A | TRP195 |
| A | THR196 |
| A | ARG197 |
| A | ASP198 |
| A | ARG228 |
| A | GAV404 |
| B | SER194 |
| B | TRP195 |
| B | THR196 |
| B | ARG197 |
| B | ASP198 |
| B | ARG228 |
| B | GAV404 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS22 |
| B | HIS79 |
| B | HIS83 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GAV B 402 |
| Chain | Residue |
| A | ARG140 |
| A | GLU209 |
| B | LEU134 |
| B | ASP165 |
| B | ILE166 |
| B | ASP167 |
| B | ARG168 |
| B | PHE169 |
| B | LYS170 |
| B | ASN173 |
| B | HIS178 |
| B | ASP182 |
| B | LEU185 |
| B | ARG204 |
| B | GLY207 |
| B | GLU208 |
| B | LYS277 |
| B | ARG281 |
| B | MG403 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 403 |
| Chain | Residue |
| B | ASP165 |
| B | ILE166 |
| B | ASP167 |
| B | GLU208 |
| B | LYS277 |
| B | GAV402 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GAV B 404 |
| Chain | Residue |
| A | C2E405 |
| B | ARG197 |
| B | TYR199 |
| B | GLU200 |
| B | LYS215 |
| B | ARG224 |
| B | ALA225 |
| B | ARG228 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255 |
| Chain | Residue | Details |
| A | GLU208 | |
| B | GLU208 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23769666, ECO:0007744|PDB:3T9O, ECO:0007744|PDB:4H54 |
| Chain | Residue | Details |
| A | HIS22 | |
| A | HIS79 | |
| A | HIS83 | |
| B | HIS22 | |
| B | HIS79 | |
| B | HIS83 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23769666, ECO:0007744|PDB:3T9O |
| Chain | Residue | Details |
| A | ALA52 | |
| B | ALA52 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23769666, ECO:0007744|PDB:4H54 |
| Chain | Residue | Details |
| A | ASP165 | |
| A | ILE166 | |
| A | GLU208 | |
| B | ASP165 | |
| B | ILE166 | |
| B | GLU208 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:23769666 |
| Chain | Residue | Details |
| A | ASN173 | |
| B | ASP182 | |
| B | TRP195 | |
| B | LYS215 | |
| B | ARG224 | |
| B | ARG228 | |
| A | HIS178 | |
| A | ASP182 | |
| A | TRP195 | |
| A | LYS215 | |
| A | ARG224 | |
| A | ARG228 | |
| B | ASN173 | |
| B | HIS178 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000255 |
| Chain | Residue | Details |
| A | LYS170 | |
| B | LYS170 |
