2AKY
HIGH-RESOLUTION STRUCTURES OF ADENYLATE KINASE FROM YEAST LIGATED WITH INHIBITOR AP5A, SHOWING THE PATHWAY OF PHOSPHORYL TRANSFER
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003688 | molecular_function | DNA replication origin binding |
| A | 0004017 | molecular_function | adenylate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0005829 | cellular_component | cytosol |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006172 | biological_process | ADP biosynthetic process |
| A | 0006270 | biological_process | DNA replication initiation |
| A | 0009117 | biological_process | nucleotide metabolic 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 | 0036388 | biological_process | pre-replicative complex assembly |
| A | 0046033 | biological_process | AMP metabolic process |
| A | 0046034 | biological_process | ATP metabolic process |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | AP5301 |
| A | HOH503 |
| A | HOH505 |
| A | HOH506 |
| site_id | AC2 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE AP5 A 301 |
| Chain | Residue |
| A | GLY18 |
| A | THR19 |
| A | THR35 |
| A | GLY36 |
| A | LEU39 |
| A | ARG40 |
| A | MET57 |
| A | GLY61 |
| A | VAL63 |
| A | MET68 |
| A | GLY90 |
| A | PHE91 |
| A | ARG93 |
| A | GLN97 |
| A | ARG128 |
| A | ARG132 |
| A | SER141 |
| A | TYR142 |
| A | HIS143 |
| A | PHE146 |
| A | ASN147 |
| A | ARG165 |
| A | ARG176 |
| A | GLN204 |
| A | PRO205 |
| A | PRO206 |
| A | MG401 |
| A | HOH502 |
| A | HOH504 |
| A | HOH506 |
| A | HOH520 |
| A | HOH523 |
| A | HOH525 |
| A | HOH531 |
| A | HOH537 |
| A | HOH548 |
| A | PRO13 |
| A | GLY14 |
| A | ALA15 |
| A | GLY16 |
| A | LYS17 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FILDGFPRtipQ |
| Chain | Residue | Details |
| A | PHE86-GLN97 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191 |
| Chain | Residue | Details |
| A | GLY14 | |
| A | ARG132 | |
| A | GLN204 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369 |
| Chain | Residue | Details |
| A | THR35 | |
| A | ARG40 | |
| A | GLY61 | |
| A | GLY90 | |
| A | GLN97 | |
| A | ARG165 | |
| A | ARG176 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191 |
| Chain | Residue | Details |
| A | SER141 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:3004985 |
| Chain | Residue | Details |
| A | SER1 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1zio |
| Chain | Residue | Details |
| A | LYS17 | |
| A | ASP167 | |
| A | ARG165 | |
| A | ARG176 | |
| A | ARG132 | |
| A | ASP168 |
