4MKF
Crystal structure of a stable adenylate kinase variant AKv3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004017 | molecular_function | AMP kinase activity |
| A | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009123 | biological_process | nucleoside monophosphate metabolic process |
| A | 0009132 | biological_process | nucleoside diphosphate metabolic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| 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 | 0044209 | biological_process | AMP salvage |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004017 | molecular_function | AMP kinase activity |
| B | 0004550 | molecular_function | nucleoside diphosphate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009123 | biological_process | nucleoside monophosphate metabolic process |
| B | 0009132 | biological_process | nucleoside diphosphate metabolic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| 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 | 0044209 | biological_process | AMP salvage |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046940 | biological_process | nucleoside monophosphate phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | CYS130 |
| A | CYS133 |
| A | CYS150 |
| A | ASP153 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | AP5303 |
| A | HOH421 |
| A | HOH445 |
| A | HOH450 |
| A | HOH589 |
| site_id | AC3 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE AP5 A 303 |
| Chain | Residue |
| A | PRO9 |
| A | GLY10 |
| A | ALA11 |
| A | GLY12 |
| A | LYS13 |
| A | GLY14 |
| A | THR15 |
| A | THR31 |
| A | GLY32 |
| A | PHE35 |
| A | ARG36 |
| A | ILE53 |
| A | GLU57 |
| A | VAL59 |
| A | THR64 |
| A | GLY85 |
| A | PHE86 |
| A | ARG88 |
| A | GLN92 |
| A | ARG123 |
| A | ARG127 |
| A | THR136 |
| A | TYR137 |
| A | HIS138 |
| A | PHE141 |
| A | ARG160 |
| A | ARG171 |
| A | GLN199 |
| A | ILE201 |
| A | MG302 |
| A | HOH416 |
| A | HOH420 |
| A | HOH421 |
| A | HOH434 |
| A | HOH435 |
| A | HOH445 |
| A | HOH449 |
| A | HOH506 |
| A | HOH507 |
| A | HOH589 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 304 |
| Chain | Residue |
| A | GLN199 |
| A | HOH459 |
| A | HOH585 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 305 |
| Chain | Residue |
| A | ASP203 |
| A | HOH628 |
| A | HOH629 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 306 |
| Chain | Residue |
| A | GLY73 |
| A | HOH517 |
| A | HOH519 |
| A | HOH591 |
| A | HOH624 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | CYS130 |
| B | CYS133 |
| B | CYS150 |
| B | ASP153 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | AP5303 |
| B | HOH421 |
| B | HOH442 |
| B | HOH443 |
| B | HOH445 |
| site_id | AC9 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE AP5 B 303 |
| Chain | Residue |
| B | HOH407 |
| B | HOH408 |
| B | HOH421 |
| B | HOH423 |
| B | HOH424 |
| B | HOH427 |
| B | HOH442 |
| B | HOH443 |
| B | HOH446 |
| B | HOH471 |
| B | HOH478 |
| B | PRO9 |
| B | GLY10 |
| B | ALA11 |
| B | GLY12 |
| B | LYS13 |
| B | GLY14 |
| B | THR15 |
| B | THR31 |
| B | GLY32 |
| B | ILE53 |
| B | GLU57 |
| B | VAL59 |
| B | THR64 |
| B | GLY85 |
| B | PHE86 |
| B | ARG88 |
| B | GLN92 |
| B | ARG123 |
| B | LEU124 |
| B | ARG127 |
| B | THR136 |
| B | TYR137 |
| B | HIS138 |
| B | PHE141 |
| B | ARG160 |
| B | ARG171 |
| B | GLY197 |
| B | GLN199 |
| B | ILE201 |
| B | MG302 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 304 |
| Chain | Residue |
| B | ASP200 |
| B | HOH627 |
| B | HOH628 |
| B | HOH629 |
| B | HOH630 |
| B | HOH631 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 305 |
| Chain | Residue |
| B | ASP200 |
| B | HOH402 |
| B | HOH473 |
| B | HOH588 |
| B | HOH592 |
| B | HOH636 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 306 |
| Chain | Residue |
| B | GLN199 |
| B | HOH587 |
| B | HOH613 |
| B | HOH614 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 307 |
| Chain | Residue |
| A | HOH436 |
| A | HOH617 |
| B | LYS40 |
| B | HOH495 |
| B | HOH586 |
| B | HOH625 |
| B | HOH626 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtvaQ |
| Chain | Residue | Details |
| A | PHE81-GLN92 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15100224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 74 |
| Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15100224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00235","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15100224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713575","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
