4I5W
Crystal structure of yeast Ap4A phosphorylase Apa2 in complex with AMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003877 | molecular_function | ATP:ADP adenylyltransferase activity |
| A | 0004780 | molecular_function | sulfate adenylyltransferase (ADP) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008796 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase activity |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0009164 | biological_process | nucleoside catabolic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033699 | molecular_function | DNA 5'-adenosine monophosphate hydrolase activity |
| B | 0003877 | molecular_function | ATP:ADP adenylyltransferase activity |
| B | 0004780 | molecular_function | sulfate adenylyltransferase (ADP) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008796 | molecular_function | bis(5'-nucleosyl)-tetraphosphatase activity |
| B | 0009117 | biological_process | nucleotide metabolic process |
| B | 0009164 | biological_process | nucleoside catabolic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033699 | molecular_function | DNA 5'-adenosine monophosphate hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 401 |
| Chain | Residue |
| A | HIS152 |
| A | HIS265 |
| A | ALA266 |
| A | LYS267 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AMP A 402 |
| Chain | Residue |
| A | MET165 |
| A | ASN277 |
| A | THR279 |
| A | MET284 |
| A | LEU286 |
| A | LYS288 |
| A | AMP403 |
| A | LEU50 |
| A | ASN92 |
| A | PHE94 |
| A | VAL96 |
| A | HIS100 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AMP A 403 |
| Chain | Residue |
| A | PRO67 |
| A | PHE68 |
| A | LEU91 |
| A | ASN92 |
| A | LYS93 |
| A | ASN148 |
| A | GLY154 |
| A | SER155 |
| A | SER156 |
| A | GLN157 |
| A | HIS161 |
| A | GLN163 |
| A | AMP402 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AMP B 401 |
| Chain | Residue |
| B | LEU75 |
| B | LEU91 |
| B | ASN92 |
| B | LYS93 |
| B | PHE94 |
| B | LEU102 |
| B | ASN148 |
| B | GLY154 |
| B | SER155 |
| B | SER156 |
| B | HIS161 |
| B | GLN163 |
| B | AMP402 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AMP B 402 |
| Chain | Residue |
| B | ASN92 |
| B | PHE94 |
| B | VAL96 |
| B | VAL97 |
| B | HIS100 |
| B | GLN163 |
| B | MET165 |
| B | THR279 |
| B | MET284 |
| B | LYS288 |
| B | AMP401 |
| B | HOH501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:23628156 |
| Chain | Residue | Details |
| A | HIS161 | |
| B | HIS161 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23628156 |
| Chain | Residue | Details |
| A | LYS53 | |
| B | ASN92 | |
| B | ASN148 | |
| B | GLY154 | |
| B | GLN163 | |
| B | ASN277 | |
| B | MET284 | |
| B | LYS288 | |
| A | ASN92 | |
| A | ASN148 | |
| A | GLY154 | |
| A | GLN163 | |
| A | ASN277 | |
| A | MET284 | |
| A | LYS288 | |
| B | LYS53 |
