2AK3
THE THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN MITOCHONDRIAL MATRIX ADENYLATE KINASE AND ITS SUBSTRATE AMP AT 1.85 ANGSTROMS RESOLUTION
Replaces: 1AK3Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004017 | molecular_function | adenylate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006172 | biological_process | ADP biosynthetic process |
| A | 0009142 | biological_process | nucleoside triphosphate biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046033 | biological_process | AMP metabolic process |
| A | 0046039 | biological_process | GTP metabolic process |
| A | 0046041 | biological_process | ITP metabolic process |
| A | 0046051 | biological_process | UTP metabolic process |
| A | 0046899 | molecular_function | nucleoside triphosphate adenylate kinase activity |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004017 | molecular_function | adenylate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0006172 | biological_process | ADP biosynthetic process |
| B | 0009142 | biological_process | nucleoside triphosphate biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016776 | molecular_function | phosphotransferase activity, phosphate group as acceptor |
| B | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0046033 | biological_process | AMP metabolic process |
| B | 0046039 | biological_process | GTP metabolic process |
| B | 0046041 | biological_process | ITP metabolic process |
| B | 0046051 | biological_process | UTP metabolic process |
| B | 0046899 | molecular_function | nucleoside triphosphate adenylate kinase activity |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 227 |
| Chain | Residue |
| A | ALA13 |
| A | GLY15 |
| A | SER16 |
| A | GLY17 |
| A | LYS18 |
| A | GLY19 |
| A | HOH324 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 227 |
| Chain | Residue |
| B | GLY17 |
| B | LYS18 |
| B | GLY19 |
| B | HOH332 |
| B | HOH392 |
| B | HOH395 |
| B | GLY15 |
| B | SER16 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AMP A 226 |
| Chain | Residue |
| A | SER36 |
| A | LEU40 |
| A | ARG41 |
| A | ILE58 |
| A | LYS62 |
| A | LEU63 |
| A | ILE64 |
| A | MET69 |
| A | GLY89 |
| A | ARG92 |
| A | GLN96 |
| A | HOH338 |
| A | HOH374 |
| A | HOH409 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AMP B 226 |
| Chain | Residue |
| B | SER36 |
| B | GLY37 |
| B | LEU40 |
| B | ARG41 |
| B | ILE58 |
| B | LYS62 |
| B | LEU63 |
| B | ILE64 |
| B | MET69 |
| B | GLY89 |
| B | ARG92 |
| B | GLN96 |
| B | HOH293 |
| B | HOH328 |
| B | HOH330 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. WLLDGFPRtlpQ |
| Chain | Residue | Details |
| A | TRP85-GLN96 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03169 |
| Chain | Residue | Details |
| A | SER16 | |
| B | ASP42 | |
| B | PHE90 | |
| B | TRP127 | |
| B | TYR136 | |
| B | GLU160 | |
| B | LEU171 | |
| B | ASN200 | |
| A | ASP42 | |
| A | PHE90 | |
| A | TRP127 | |
| A | TYR136 | |
| A | GLU160 | |
| A | LEU171 | |
| A | ASN200 | |
| B | SER16 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:1994037 |
| Chain | Residue | Details |
| A | GLY37 | |
| A | LEU63 | |
| A | ALA97 | |
| B | GLY37 | |
| B | LEU63 | |
| B | ALA97 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WTP7 |
| Chain | Residue | Details |
| A | GLY19 | |
| A | THR56 | |
| B | GLY19 | |
| B | THR56 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 |
| Chain | Residue | Details |
| A | HIS28 | |
| B | LYS188 | |
| A | LEU63 | |
| A | ASN79 | |
| A | ALA173 | |
| A | LYS188 | |
| B | HIS28 | |
| B | LEU63 | |
| B | ASN79 | |
| B | ALA173 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9WTP7 |
| Chain | Residue | Details |
| A | HIS33 | |
| A | ILE202 | |
| B | HIS33 | |
| B | ILE202 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WTP7 |
| Chain | Residue | Details |
| A | SER36 | |
| B | SER36 |
