4FE2
X-Ray Structure of SAICAR Synthetase (PurC) from Streptococcus pneumoniae complexed with AIR, ADP, Asp and Mg2+
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004639 | molecular_function | phosphoribosylaminoimidazolesuccinocarboxamide synthase 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 | 0009236 | biological_process | cobalamin biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
B | 0004639 | molecular_function | phosphoribosylaminoimidazolesuccinocarboxamide synthase 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 | 0009236 | biological_process | cobalamin biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AIR A 301 |
Chain | Residue |
A | ARG93 |
A | ARG214 |
A | ASP306 |
A | HOH402 |
A | HOH412 |
A | HOH495 |
A | HOH555 |
A | GLY98 |
A | SER99 |
A | ASP174 |
A | LYS176 |
A | ASP196 |
A | ASN197 |
A | CYS198 |
A | ARG199 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP A 302 |
Chain | Residue |
A | TYR7 |
A | GLY9 |
A | LYS10 |
A | ALA11 |
A | LYS12 |
A | ILE14 |
A | HIS68 |
A | LYS81 |
A | VAL83 |
A | ILE85 |
A | LYS122 |
A | GLU178 |
A | ASP191 |
A | MG303 |
A | ASP306 |
A | HOH505 |
A | HOH506 |
A | HOH517 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 303 |
Chain | Residue |
A | ADP302 |
A | ASP306 |
A | HOH504 |
A | HOH505 |
A | HOH506 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 144 A 304 |
Chain | Residue |
A | ASN61 |
A | VAL62 |
A | GLY64 |
A | HOH559 |
A | HOH601 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 305 |
Chain | Residue |
A | ARG103 |
B | ARG103 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ASP A 306 |
Chain | Residue |
A | LYS10 |
A | GLU89 |
A | LYS176 |
A | ASP191 |
A | ASN197 |
A | AIR301 |
A | ADP302 |
A | MG303 |
A | HOH504 |
A | HOH505 |
A | HOH535 |
A | HOH555 |
A | HOH571 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 144 A 307 |
Chain | Residue |
A | ALA63 |
A | GLY64 |
A | GLU153 |
A | ARG156 |
A | HOH579 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 144 A 308 |
Chain | Residue |
A | ASN94 |
A | TYR95 |
A | ALA111 |
A | LEU112 |
A | GLU113 |
A | HOH523 |
A | HOH537 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AIR B 301 |
Chain | Residue |
B | GLU89 |
B | ARG93 |
B | ALA97 |
B | SER99 |
B | ASP174 |
B | LYS176 |
B | ASP196 |
B | ASN197 |
B | CYS198 |
B | ARG199 |
B | ARG214 |
B | HOH403 |
B | HOH406 |
B | HOH487 |
B | HOH512 |
site_id | BC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADP B 302 |
Chain | Residue |
B | HOH475 |
B | HOH556 |
B | TYR7 |
B | GLY9 |
B | LYS10 |
B | ALA11 |
B | LYS12 |
B | ILE14 |
B | HIS68 |
B | LYS81 |
B | VAL83 |
B | ILE85 |
B | GLU178 |
B | ASP191 |
B | MG303 |
B | HOH415 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 303 |
Chain | Residue |
B | ADP302 |
B | HOH415 |
B | HOH508 |
B | HOH509 |
B | HOH556 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 144 B 304 |
Chain | Residue |
A | LYS102 |
A | ARG103 |
B | LEU126 |
B | ASP127 |
B | PRO129 |
B | HOH532 |
B | HOH543 |
B | HOH555 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 305 |
Chain | Residue |
B | ASN94 |
B | TYR95 |
B | ALA111 |
B | LEU112 |
B | HOH542 |
Functional Information from PROSITE/UniProt