4W5J
New structural conformations of adenylate kinase from Streptococcus pneumoniae D39 with Ap5A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004017 | molecular_function | adenylate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| A | 0044209 | biological_process | AMP salvage |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| A | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
| B | 0004017 | molecular_function | adenylate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| B | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| B | 0044209 | biological_process | AMP salvage |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| B | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
| C | 0004017 | molecular_function | adenylate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| C | 0009165 | biological_process | nucleotide biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| C | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| C | 0044209 | biological_process | AMP salvage |
| C | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| C | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
| D | 0004017 | molecular_function | adenylate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| D | 0009165 | biological_process | nucleotide biosynthetic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| D | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| D | 0044209 | biological_process | AMP salvage |
| D | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| D | 0050145 | molecular_function | nucleoside monophosphate kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | AP5302 |
| A | HOH506 |
| A | HOH508 |
| A | HOH512 |
| A | HOH527 |
| site_id | AC2 |
| Number of Residues | 39 |
| Details | binding site for residue AP5 A 302 |
| Chain | Residue |
| A | LYS13 |
| A | GLY14 |
| A | THR15 |
| A | THR31 |
| A | GLY32 |
| A | PHE35 |
| A | ARG36 |
| A | ILE53 |
| A | GLU57 |
| A | VAL59 |
| A | THR64 |
| A | GLY86 |
| A | TYR87 |
| A | ARG89 |
| A | GLN93 |
| A | ARG124 |
| A | ARG128 |
| A | THR137 |
| A | PHE138 |
| A | HIS139 |
| A | PHE142 |
| A | ARG156 |
| A | ARG167 |
| A | GLN195 |
| A | ILE197 |
| A | MG301 |
| A | HOH450 |
| A | HOH499 |
| A | HOH500 |
| A | HOH501 |
| A | HOH505 |
| A | HOH506 |
| A | HOH508 |
| A | HOH521 |
| A | HOH522 |
| A | PRO9 |
| A | GLY10 |
| A | ALA11 |
| A | GLY12 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | AP5302 |
| B | HOH480 |
| B | HOH482 |
| B | HOH492 |
| B | HOH497 |
| site_id | AC4 |
| Number of Residues | 39 |
| Details | binding site for residue AP5 B 302 |
| Chain | Residue |
| B | PRO9 |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| B | GLY14 |
| B | THR15 |
| B | THR31 |
| B | GLY32 |
| B | PHE35 |
| B | ARG36 |
| B | ILE53 |
| B | GLU57 |
| B | LEU58 |
| B | VAL59 |
| B | THR64 |
| B | GLY86 |
| B | TYR87 |
| B | ARG89 |
| B | GLN93 |
| B | ARG124 |
| B | ARG128 |
| B | THR137 |
| B | PHE138 |
| B | HIS139 |
| B | PHE142 |
| B | ARG156 |
| B | ARG167 |
| B | GLN195 |
| B | ILE197 |
| B | MG301 |
| B | HOH439 |
| B | HOH477 |
| B | HOH478 |
| B | HOH479 |
| B | HOH480 |
| B | HOH482 |
| B | HOH491 |
| B | HOH511 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 301 |
| Chain | Residue |
| C | AP5302 |
| C | HOH502 |
| C | HOH510 |
| C | HOH516 |
| C | HOH528 |
| site_id | AC6 |
| Number of Residues | 42 |
| Details | binding site for residue AP5 C 302 |
| Chain | Residue |
| C | THR15 |
| C | THR31 |
| C | GLY32 |
| C | PHE35 |
| C | ARG36 |
| C | ILE53 |
| C | GLU57 |
| C | LEU58 |
| C | VAL59 |
| C | THR64 |
| C | GLY86 |
| C | TYR87 |
| C | ARG89 |
| C | GLN93 |
| C | ARG124 |
| C | ARG128 |
| C | THR137 |
| C | PHE138 |
| C | HIS139 |
| C | PHE142 |
| C | ARG156 |
| C | ARG167 |
| C | GLN195 |
| C | ILE197 |
| C | MG301 |
| C | HOH425 |
| C | HOH494 |
| C | HOH495 |
| C | HOH496 |
| C | HOH497 |
| C | HOH502 |
| C | HOH504 |
| C | HOH510 |
| C | HOH516 |
| C | HOH525 |
| C | HOH589 |
| C | PRO9 |
| C | GLY10 |
| C | ALA11 |
| C | GLY12 |
| C | LYS13 |
| C | GLY14 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 301 |
| Chain | Residue |
| D | AP5302 |
| D | HOH506 |
| D | HOH514 |
| D | HOH575 |
| site_id | AC8 |
| Number of Residues | 40 |
| Details | binding site for residue AP5 D 302 |
| Chain | Residue |
| D | PRO9 |
| D | GLY10 |
| D | ALA11 |
| D | GLY12 |
| D | LYS13 |
| D | GLY14 |
| D | THR15 |
| D | THR31 |
| D | GLY32 |
| D | PHE35 |
| D | ARG36 |
| D | ILE53 |
| D | GLU57 |
| D | LEU58 |
| D | VAL59 |
| D | THR64 |
| D | GLY86 |
| D | TYR87 |
| D | ARG89 |
| D | GLN93 |
| D | ARG124 |
| D | ARG128 |
| D | THR137 |
| D | PHE138 |
| D | HIS139 |
| D | PHE142 |
| D | ARG156 |
| D | ARG167 |
| D | GLN195 |
| D | ILE197 |
| D | MG301 |
| D | HOH430 |
| D | HOH486 |
| D | HOH487 |
| D | HOH489 |
| D | HOH490 |
| D | HOH495 |
| D | HOH506 |
| D | HOH512 |
| D | HOH531 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLLDGYPRtieQ |
| Chain | Residue | Details |
| A | PHE82-GLN93 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235 |
| Chain | Residue | Details |
| A | GLY10 | |
| A | ARG167 | |
| A | GLN195 | |
| B | GLY10 | |
| B | THR31 | |
| B | ARG36 | |
| B | GLU57 | |
| B | GLY86 | |
| B | GLN93 | |
| B | ARG128 | |
| B | THR137 | |
| A | THR31 | |
| B | ARG156 | |
| B | ARG167 | |
| B | GLN195 | |
| C | GLY10 | |
| C | THR31 | |
| C | ARG36 | |
| C | GLU57 | |
| C | GLY86 | |
| C | GLN93 | |
| C | ARG128 | |
| A | ARG36 | |
| C | THR137 | |
| C | ARG156 | |
| C | ARG167 | |
| C | GLN195 | |
| D | GLY10 | |
| D | THR31 | |
| D | ARG36 | |
| D | GLU57 | |
| D | GLY86 | |
| D | GLN93 | |
| A | GLU57 | |
| D | ARG128 | |
| D | THR137 | |
| D | ARG156 | |
| D | ARG167 | |
| D | GLN195 | |
| A | GLY86 | |
| A | GLN93 | |
| A | ARG128 | |
| A | THR137 | |
| A | ARG156 |
