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 |