4U0M
Structure of the Vibrio cholerae di-nucleotide cyclase (DncV) mutant D193N in complex with ATP, GTP and 5MTHFGLU2
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 | 22 |
| Details | binding site for residue GTP A 501 |
| Chain | Residue |
| A | GLN112 |
| A | ASP348 |
| A | LEU352 |
| A | ATP502 |
| A | MG503 |
| A | HOH656 |
| A | HOH681 |
| A | HOH685 |
| A | HOH689 |
| A | HOH692 |
| A | HOH699 |
| A | GLY113 |
| A | HOH720 |
| A | HOH763 |
| A | HOH774 |
| A | SER114 |
| A | TYR117 |
| A | ASP131 |
| A | ASP133 |
| A | VAL264 |
| A | LYS287 |
| A | SER301 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue ATP A 502 |
| Chain | Residue |
| A | GLN112 |
| A | ASP133 |
| A | LYS177 |
| A | THR179 |
| A | ARG182 |
| A | ASN193 |
| A | LEU247 |
| A | SER259 |
| A | GTP501 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 503 |
| Chain | Residue |
| A | ASP131 |
| A | ASP133 |
| A | GTP501 |
| A | HOH763 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue TLL A 504 |
| Chain | Residue |
| A | ARG36 |
| A | ARG40 |
| A | ARG44 |
| A | ARG108 |
| A | PHE109 |
| A | TRP110 |
| A | THR111 |
| A | GLN116 |
| A | TYR137 |
| A | PHE204 |
| A | GLN208 |
| A | GLU239 |
| A | LEU240 |
| A | ASP260 |
| A | PRO261 |
| A | LYS262 |
| A | HOH760 |
| A | HOH787 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue GTP B 501 |
| Chain | Residue |
| B | GLN112 |
| B | GLY113 |
| B | SER114 |
| B | TYR117 |
| B | ASP131 |
| B | ASP133 |
| B | VAL264 |
| B | LYS287 |
| B | SER301 |
| B | ASP345 |
| B | ASP348 |
| B | LEU352 |
| B | ATP502 |
| B | MG503 |
| B | HOH649 |
| B | HOH668 |
| B | HOH678 |
| B | HOH685 |
| B | HOH708 |
| B | HOH724 |
| B | HOH730 |
| B | HOH739 |
| B | HOH765 |
| B | HOH766 |
| B | HOH778 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue ATP B 502 |
| Chain | Residue |
| B | ASP131 |
| B | ASP133 |
| B | LYS177 |
| B | THR179 |
| B | ARG182 |
| B | HIS191 |
| B | ASN193 |
| B | SER259 |
| B | GTP501 |
| B | HOH695 |
| B | HOH702 |
| B | HOH708 |
| B | HOH739 |
| B | HOH762 |
| B | HOH776 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | ASP131 |
| B | ASP133 |
| B | GTP501 |
| B | HOH724 |
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 | SER301 | |
| B | GLN112 | |
| B | LYS287 | |
| B | SER301 | |
| A | GLN112 | |
| A | LYS287 |
| 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 | ASP131 | |
| A | ASP133 | |
| A | ASN193 | |
| B | ASP131 | |
| B | ASP133 | |
| B | ASN193 |
| 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 | ARG182 | |
| B | ARG182 |
| 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 | SER259 | |
| B | SER259 |
| 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 | ASP348 | |
| B | ASP348 |
