4TY0
Crystal structure of Vibrio cholerae DncV cyclic AMP-GMP synthase in complex with linear intermediate 5' pppA(3',5')pG
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005575 | cellular_component | cellular_component |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| A | 0009405 | biological_process | obsolete pathogenesis |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050922 | biological_process | negative regulation of chemotaxis |
| A | 0051607 | biological_process | defense response to virus |
| A | 0052621 | molecular_function | diguanylate cyclase activity |
| A | 0140701 | molecular_function | 3',3'-cyclic GMP-AMP synthase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005575 | cellular_component | cellular_component |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
| B | 0009405 | biological_process | obsolete pathogenesis |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050922 | biological_process | negative regulation of chemotaxis |
| B | 0051607 | biological_process | defense response to virus |
| B | 0052621 | molecular_function | diguanylate cyclase activity |
| B | 0140701 | molecular_function | 3',3'-cyclic GMP-AMP synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 501 |
| Chain | Residue |
| A | ASP132 |
| A | ASP134 |
| A | ASP194 |
| A | 38V503 |
| A | HOH678 |
| A | HOH679 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | HOH680 |
| A | ASP132 |
| A | ASP134 |
| A | 38V503 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | binding site for residue 38V A 503 |
| Chain | Residue |
| A | GLN113 |
| A | GLY114 |
| A | SER115 |
| A | TYR118 |
| A | ASP132 |
| A | ASP134 |
| A | LYS178 |
| A | THR180 |
| A | CYS181 |
| A | ASP194 |
| A | TYR198 |
| A | SER260 |
| A | PRO262 |
| A | LYS288 |
| A | SER302 |
| A | LEU353 |
| A | MG501 |
| A | MG502 |
| A | HOH679 |
| A | HOH680 |
| A | HOH681 |
| A | HOH697 |
| A | HOH718 |
| A | HOH730 |
| A | HOH731 |
| A | HOH766 |
| A | HOH767 |
| A | HOH768 |
| A | HOH773 |
| A | HOH778 |
| A | HOH794 |
| A | HOH807 |
| A | HOH855 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 504 |
| Chain | Residue |
| A | TRP111 |
| A | TYR138 |
| A | PHE205 |
| A | LYS263 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue ACT A 505 |
| Chain | Residue |
| A | PHE125 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue ACT A 506 |
| Chain | Residue |
| A | GLU343 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 501 |
| Chain | Residue |
| B | ASP132 |
| B | ASP134 |
| B | ASP194 |
| B | MG502 |
| B | 38V503 |
| B | HOH681 |
| B | HOH682 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | ASP132 |
| B | ASP134 |
| B | MG501 |
| B | 38V503 |
| B | HOH683 |
| site_id | AC9 |
| Number of Residues | 36 |
| Details | binding site for residue 38V B 503 |
| Chain | Residue |
| B | GLN113 |
| B | GLY114 |
| B | SER115 |
| B | TYR118 |
| B | ASP132 |
| B | ASP134 |
| B | LYS178 |
| B | THR180 |
| B | CYS181 |
| B | ASP194 |
| B | PRO196 |
| B | TYR198 |
| B | SER260 |
| B | PRO262 |
| B | LYS288 |
| B | SER302 |
| B | LEU353 |
| B | MG501 |
| B | MG502 |
| B | HOH682 |
| B | HOH683 |
| B | HOH695 |
| B | HOH698 |
| B | HOH716 |
| B | HOH754 |
| B | HOH758 |
| B | HOH767 |
| B | HOH770 |
| B | HOH771 |
| B | HOH772 |
| B | HOH775 |
| B | HOH778 |
| B | HOH790 |
| B | HOH794 |
| B | HOH833 |
| B | HOH841 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25131990, ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248, ECO:0007744|PDB:4U03, ECO:0007744|PDB:4U0M, ECO:0007744|PDB:4XJ3, ECO:0007744|PDB:4XJ4, ECO:0007744|PDB:4XJ5 |
| Chain | Residue | Details |
| A | GLN113 | |
| A | LYS288 | |
| A | SER302 | |
| B | GLN113 | |
| B | LYS288 | |
| B | SER302 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25131990, ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248, ECO:0007744|PDB:4TXY, ECO:0007744|PDB:4TXZ, ECO:0007744|PDB:4TY0, ECO:0007744|PDB:4U03, ECO:0007744|PDB:4U0N, ECO:0007744|PDB:4XJ5 |
| Chain | Residue | Details |
| A | ASP132 | |
| A | ASP134 | |
| A | ASP194 | |
| B | ASP132 | |
| B | ASP134 | |
| B | ASP194 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25131990, ECO:0000269|PubMed:25201413, ECO:0007744|PDB:4U0M |
| Chain | Residue | Details |
| A | ARG183 | |
| B | ARG183 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25131990, ECO:0000269|PubMed:25201413, ECO:0007744|PDB:4U03, ECO:0007744|PDB:4XJ3, ECO:0007744|PDB:4XJ4, ECO:0007744|PDB:4XJ5 |
| Chain | Residue | Details |
| A | SER260 | |
| B | SER260 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25131990, ECO:0000269|PubMed:25201413, ECO:0000269|PubMed:25865248, ECO:0007744|PDB:4U03, ECO:0007744|PDB:4U0M, ECO:0007744|PDB:4XJ3, ECO:0007744|PDB:4XJ5 |
| Chain | Residue | Details |
| A | ASP349 | |
| B | ASP349 |
