2JDX
CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE, DELETIONMUTANT ATDELTAM302
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0006600 | biological_process | creatine metabolic process |
| A | 0006601 | biological_process | creatine biosynthetic process |
| A | 0007611 | biological_process | learning or memory |
| A | 0014889 | biological_process | muscle atrophy |
| A | 0015067 | molecular_function | amidinotransferase activity |
| A | 0015068 | molecular_function | glycine amidinotransferase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
Functional Information from PROSITE/UniProt
| site_id | PS00430 |
| Number of Residues | 61 |
| Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. stqaatassrnscaaddkateplpkdcpvssynewdpleevivgraenacvpp..............................................................FTIEVKAN |
| Chain | Residue | Details |
| A | SER38-ASN98 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"9218780","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JDW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Amidino-cysteine intermediate","evidences":[{"source":"PubMed","id":"9148748","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9218780","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JDW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9218780","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4JDW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1bwd |
| Chain | Residue | Details |
| A | HIS406 | |
| A | ASP254 | |
| A | ASP170 | |
| A | ARG189 | |
| A | CYS407 | |
| A | ASP305 | |
| A | HIS303 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bwd |
| Chain | Residue | Details |
| A | ASP254 | |
| A | CYS407 | |
| A | HIS303 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 18 |
| Chain | Residue | Details |
| A | ASP170 | electrostatic stabiliser, hydrogen bond acceptor |
| A | ASP254 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS303 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP305 | electrostatic stabiliser, hydrogen bond acceptor |
| A | CYS407 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
