Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009190 | biological_process | cyclic nucleotide biosynthetic process |
A | 0016849 | molecular_function | phosphorus-oxygen lyase activity |
A | 0035556 | biological_process | intracellular signal transduction |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue EDO A 501 |
Chain | Residue |
A | ILE243 |
A | ALA244 |
A | ASP245 |
A | ARG278 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | HOH684 |
A | SER306 |
A | GLY307 |
A | VAL308 |
A | PRO309 |
A | ARG310 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | LEU324 |
A | THR327 |
A | ASN328 |
A | GLY384 |
A | GLN385 |
A | ILE422 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | ARG278 |
A | PRO309 |
A | LEU333 |
A | LYS334 |
A | EDO507 |
A | HOH606 |
A | HOH645 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | ASP256 |
A | GLY259 |
A | GLU285 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | ASP288 |
A | GLN289 |
A | GLY291 |
A | ARG344 |
A | SER379 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | ALA244 |
A | ASP245 |
A | TYR247 |
A | ARG278 |
A | ALA354 |
A | GLY355 |
A | TYR364 |
A | EDO504 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | LYS246 |
A | TYR247 |
A | ASP248 |
A | HOH691 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | ASP284 |
A | ASP288 |
A | HOH615 |
A | HOH658 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 510 |
Chain | Residue |
A | ARG376 |
A | PRO389 |
A | ASP390 |
A | ARG417 |
A | HOH631 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue EDO A 511 |
Chain | Residue |
A | PRO311 |
A | ARG376 |
A | HOH610 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 512 |
Chain | Residue |
A | ARG310 |
A | PRO311 |
A | ARG312 |
A | HOH684 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 513 |
Chain | Residue |
A | TYR393 |
A | LYS397 |
A | PHE400 |
A | VAL401 |
A | LEU402 |
A | HOH657 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 514 |
Chain | Residue |
A | GLN387 |
A | ARG405 |
A | GLY406 |
A | MET416 |
A | THR418 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 515 |
Chain | Residue |
A | VAL297 |
A | MET303 |
A | ARG337 |
A | ASP365 |
A | VAL366 |
A | VAL371 |
A | HOH623 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue EDO A 516 |
Chain | Residue |
A | GLU239 |
A | ASN241 |
A | ASP335 |
A | ASN339 |
A | EDO518 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue EDO A 517 |
Chain | Residue |
A | ASP277 |
A | TYR280 |
A | SER281 |
A | ASP284 |
A | LYS294 |
A | HOH677 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue EDO A 518 |
Chain | Residue |
A | ASN241 |
A | ARG337 |
A | TRP367 |
A | EDO516 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue PEG A 519 |
Chain | Residue |
A | GLN289 |
A | HIS290 |
A | ARG344 |
A | SER379 |
A | ASP381 |
A | HOH607 |
site_id | AE2 |
Number of Residues | 3 |
Details | binding site for residue GOL A 520 |
Chain | Residue |
A | GLY423 |
A | ARG424 |
A | ASN328 |
Functional Information from PROSITE/UniProt
site_id | PS00452 |
Number of Residues | 24 |
Details | GUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVV.GsrrfrYdVWGDAVNvasrmE |
Chain | Residue | Details |
A | GLY355-GLU378 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP256 | |
A | ASP300 | |