4DLK
Crystal Structure of ATP-Ca++ complex of purK: N5-carboxyaminoimidazole ribonucleotide synthetase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase 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 | 0016829 | molecular_function | lyase activity |
A | 0016874 | molecular_function | ligase activity |
A | 0034028 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide synthase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051287 | molecular_function | NAD binding |
B | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase 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 | 0016829 | molecular_function | lyase activity |
B | 0016874 | molecular_function | ligase activity |
B | 0034028 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide synthase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 401 |
Chain | Residue |
A | GLU268 |
A | ATP404 |
A | HOH526 |
A | HOH529 |
A | HOH549 |
A | HOH561 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 402 |
Chain | Residue |
A | ATP405 |
A | HOH534 |
A | HOH537 |
A | HOH561 |
A | GLU255 |
A | GLU268 |
A | ATP404 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 403 |
Chain | Residue |
A | ASP154 |
A | ATP404 |
A | ATP405 |
A | HOH533 |
A | HOH543 |
A | HOH551 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE ATP A 404 |
Chain | Residue |
A | ARG107 |
A | LYS147 |
A | ASP154 |
A | GLY155 |
A | GLN158 |
A | GLU182 |
A | LYS183 |
A | TRP184 |
A | VAL185 |
A | PHE187 |
A | GLU190 |
A | PHE257 |
A | ASN267 |
A | GLU268 |
A | CA401 |
A | CA402 |
A | CA403 |
A | ATP405 |
A | HOH526 |
A | HOH529 |
A | HOH534 |
A | HOH537 |
A | HOH539 |
A | HOH543 |
A | HOH558 |
A | HOH570 |
A | HOH622 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ATP A 405 |
Chain | Residue |
A | GLU76 |
A | TYR153 |
A | HIS213 |
A | GLU255 |
A | ARG272 |
A | HIS274 |
A | ASN275 |
A | LYS348 |
A | CA402 |
A | CA403 |
A | ATP404 |
A | ATP406 |
A | HOH505 |
A | HOH517 |
A | HOH533 |
A | HOH535 |
A | HOH543 |
A | HOH545 |
A | HOH561 |
A | HOH584 |
A | HOH619 |
A | HOH627 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ATP A 406 |
Chain | Residue |
A | PHE77 |
A | LYS340 |
A | ARG347 |
A | ATP405 |
A | HOH542 |
A | HOH556 |
A | HOH604 |
A | HOH619 |
A | HOH646 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 407 |
Chain | Residue |
A | ALA46 |
A | GLN47 |
A | VAL48 |
A | ALA49 |
B | GLN47 |
B | VAL48 |
B | ALA49 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 401 |
Chain | Residue |
B | GLU255 |
B | GLU268 |
B | ATP403 |
B | HOH550 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 402 |
Chain | Residue |
B | GLY152 |
B | GLU268 |
B | ATP403 |
site_id | BC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE ATP B 403 |
Chain | Residue |
B | GLU182 |
B | LYS183 |
B | TRP184 |
B | VAL185 |
B | PHE187 |
B | GLU190 |
B | HIS213 |
B | ASN216 |
B | GLU255 |
B | PHE257 |
B | ASN267 |
B | GLU268 |
B | CA401 |
B | CA402 |
B | HOH510 |
B | HOH561 |
B | HOH583 |
B | HOH606 |
B | HOH623 |
B | ARG107 |
B | VAL145 |
B | LYS147 |
B | GLY152 |
B | TYR153 |
B | ASP154 |
B | GLY155 |
B | GLN158 |