5VEV
Crystal Structure of Phosphoribosylamine-glycine Ligase from Neisseria gonorrhoeae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004637 | molecular_function | phosphoribosylamine-glycine ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0009113 | biological_process | purine nucleobase biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004637 | molecular_function | phosphoribosylamine-glycine ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0009113 | biological_process | purine nucleobase biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue NA A 501 |
| Chain | Residue |
| A | ASP212 |
| A | LYS214 |
| A | GLY226 |
| A | ARG288 |
| A | ASP291 |
| A | PRO292 |
| A | GLU293 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 502 |
| Chain | Residue |
| A | ASP353 |
| A | GLY351 |
| A | LEU352 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 503 |
| Chain | Residue |
| A | ASN202 |
| A | LYS258 |
| A | EDO504 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | ASN202 |
| A | HIS203 |
| A | ACT503 |
| A | EDO505 |
| A | HOH626 |
| B | ASN202 |
| B | HIS203 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | ASN202 |
| A | HIS203 |
| A | EDO504 |
| A | HOH696 |
| B | HIS203 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | ALA208 |
| A | ARG300 |
| A | HOH615 |
| A | HOH689 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | ALA31 |
| A | LEU48 |
| A | THR49 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | TRP17 |
| A | GLN21 |
| A | LYS360 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | GLN337 |
| A | ASP408 |
| B | HIS262 |
| B | EDO505 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 510 |
| Chain | Residue |
| A | GLU243 |
| A | ARG244 |
| A | ASN247 |
| A | GLU248 |
| A | HOH682 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 511 |
| Chain | Residue |
| A | GLY379 |
| A | ARG380 |
| A | HOH604 |
| A | HOH606 |
| A | HOH627 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue NA B 501 |
| Chain | Residue |
| B | ASP212 |
| B | LYS214 |
| B | GLY226 |
| B | ARG288 |
| B | ASP291 |
| B | PRO292 |
| B | GLU293 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue ACT B 502 |
| Chain | Residue |
| B | TRP17 |
| B | LYS360 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| A | LYS321 |
| B | MET207 |
| B | THR209 |
| B | TYR242 |
| B | HOH626 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | CYS58 |
| B | ASN62 |
| B | ILE63 |
| B | HOH670 |
| B | HOH702 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| A | EDO509 |
| B | GLN94 |
| B | GLN98 |
| B | HOH613 |
| B | HOH672 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | THR238 |
| B | ALA240 |
| B | VAL241 |
| B | GLY278 |
| B | HOH679 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| B | ASN45 |
| B | THR367 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 508 |
| Chain | Residue |
| B | ARG244 |
| B | ASN247 |
| B | GLU248 |
| B | HOH604 |
| B | HOH621 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 509 |
| Chain | Residue |
| B | PHE105 |
| B | GLU260 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 510 |
| Chain | Residue |
| B | TYR339 |
| B | ARG380 |
| B | HOH610 |
| B | HOH619 |
Functional Information from PROSITE/UniProt
| site_id | PS00184 |
| Number of Residues | 8 |
| Details | GARS Phosphoribosylglycinamide synthetase signature. RFGDPEtQ |
| Chain | Residue | Details |
| A | ARG288-GLN295 |
