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 |