6ZJE
Crystal structure of human adenylate kinase 3, AK3, in complex with inhibitor Ap5A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004017 | molecular_function | AMP kinase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0007596 | biological_process | blood coagulation |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0009123 | biological_process | nucleoside monophosphate metabolic process |
| A | 0009142 | biological_process | nucleoside triphosphate 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 | 0016874 | molecular_function | ligase activity |
| A | 0019205 | molecular_function | nucleobase-containing compound kinase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 40 |
| Details | binding site for residue AP5 A 401 |
| Chain | Residue |
| A | PRO16 |
| A | LEU65 |
| A | ILE66 |
| A | MET71 |
| A | GLY91 |
| A | ARG94 |
| A | GLN98 |
| A | ARG124 |
| A | LEU125 |
| A | ARG172 |
| A | THR201 |
| A | GLY17 |
| A | CL402 |
| A | MG405 |
| A | HOH501 |
| A | HOH503 |
| A | HOH504 |
| A | HOH511 |
| A | HOH512 |
| A | HOH541 |
| A | HOH545 |
| A | HOH553 |
| A | GLY21 |
| A | HOH575 |
| A | HOH613 |
| A | HOH663 |
| A | HOH665 |
| A | HOH692 |
| A | HOH694 |
| A | HOH717 |
| A | HOH725 |
| A | HOH733 |
| A | HOH748 |
| A | SER38 |
| A | HOH766 |
| A | GLY39 |
| A | LEU42 |
| A | ARG43 |
| A | ILE60 |
| A | LYS64 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | GLY17 |
| A | SER18 |
| A | GLY19 |
| A | LYS20 |
| A | GLY21 |
| A | AP5401 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | ARG128 |
| A | ASN139 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 404 |
| Chain | Residue |
| A | ASN143 |
| A | HOH547 |
| A | HOH552 |
| A | HOH643 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 405 |
| Chain | Residue |
| A | AP5401 |
| A | HOH541 |
| A | HOH545 |
| A | HOH607 |
| A | HOH631 |
| A | HOH665 |
| A | HOH731 |
Functional Information from PROSITE/UniProt
| site_id | PS00113 |
| Number of Residues | 12 |
| Details | ADENYLATE_KINASE Adenylate kinase signature. WLLDGFPRtlpQ |
| Chain | Residue | Details |
| A | TRP87-GLN98 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 29 |
| Details | Region: {"description":"NMP","evidences":[{"source":"HAMAP-Rule","id":"MF_03169","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2005","submissionDatabase":"PDB data bank","title":"Structure of human adenylate kinase 3-like 1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 37 |
| Details | Region: {"description":"LID","evidences":[{"source":"HAMAP-Rule","id":"MF_03169","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2005","submissionDatabase":"PDB data bank","title":"Structure of human adenylate kinase 3-like 1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32822537","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6ZJB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P08760","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WTP7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
