3CR7
Crystal structure of N-terminal truncation of APS Kinase from Penicillium chrysogenum: Ternary structure with ADP and PAPS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0004020 | molecular_function | adenylylsulfate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0019344 | biological_process | cysteine biosynthetic process |
| A | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0004020 | molecular_function | adenylylsulfate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0019344 | biological_process | cysteine biosynthetic process |
| B | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| C | 0000103 | biological_process | sulfate assimilation |
| C | 0004020 | molecular_function | adenylylsulfate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0009086 | biological_process | methionine biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0019344 | biological_process | cysteine biosynthetic process |
| C | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| D | 0000103 | biological_process | sulfate assimilation |
| D | 0004020 | molecular_function | adenylylsulfate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0009086 | biological_process | methionine biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0019344 | biological_process | cysteine biosynthetic process |
| D | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 503 |
| Chain | Residue |
| A | LYS156 |
| A | HOH2038 |
| D | TYR172 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 502 |
| Chain | Residue |
| B | SER107 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 501 |
| Chain | Residue |
| B | TYR172 |
| C | LYS156 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP A 2001 |
| Chain | Residue |
| A | GLY37 |
| A | LYS38 |
| A | SER39 |
| A | THR40 |
| A | ARG148 |
| A | PRO150 |
| A | LEU187 |
| A | HOH2052 |
| A | HOH2085 |
| A | HOH2098 |
| C | GLU186 |
| A | SER34 |
| A | ALA35 |
| A | SER36 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PPS A 2002 |
| Chain | Residue |
| A | ARG66 |
| A | PHE75 |
| A | ARG80 |
| A | ASN83 |
| A | PHE105 |
| A | ILE106 |
| A | SER107 |
| A | PRO108 |
| A | LYS151 |
| A | LEU153 |
| A | ILE162 |
| A | LYS163 |
| A | GLU164 |
| A | PHE165 |
| A | THR166 |
| A | HOH2018 |
| A | HOH2042 |
| A | HOH2098 |
| A | HOH2109 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP B 2003 |
| Chain | Residue |
| B | SER34 |
| B | ALA35 |
| B | SER36 |
| B | GLY37 |
| B | LYS38 |
| B | SER39 |
| B | THR40 |
| B | ARG148 |
| B | PRO150 |
| B | ASN184 |
| B | LEU187 |
| B | VAL189 |
| B | HOH2004 |
| B | HOH2119 |
| D | ARG148 |
| D | ADP2006 |
| D | HOH2111 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP C 2004 |
| Chain | Residue |
| A | GLU186 |
| C | SER34 |
| C | ALA35 |
| C | SER36 |
| C | GLY37 |
| C | LYS38 |
| C | SER39 |
| C | THR40 |
| C | ARG148 |
| C | PRO150 |
| C | LYS151 |
| C | ASN184 |
| C | LEU187 |
| C | HOH2086 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PPS C 2005 |
| Chain | Residue |
| C | ARG66 |
| C | PHE75 |
| C | ARG80 |
| C | ASN83 |
| C | ILE84 |
| C | PHE105 |
| C | ILE106 |
| C | SER107 |
| C | PRO108 |
| C | LEU153 |
| C | LYS163 |
| C | GLU164 |
| C | PHE165 |
| C | THR166 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP D 2006 |
| Chain | Residue |
| D | HOH2039 |
| D | HOH2111 |
| B | ARG148 |
| B | ADP2003 |
| B | HOH2004 |
| D | LEU33 |
| D | ALA35 |
| D | SER36 |
| D | GLY37 |
| D | LYS38 |
| D | SER39 |
| D | THR40 |
| D | ARG148 |
| D | ASN184 |
| D | LEU187 |
| D | HOH2010 |
| D | HOH2012 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Phosphoserine intermediate => ECO:0000250 |
| Chain | Residue | Details |
| A | SER107 | |
| B | SER107 | |
| C | SER107 | |
| D | SER107 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY32 | |
| B | GLY32 | |
| C | GLY32 | |
| D | GLY32 |
