8JDW
CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH L-ALANINE
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 PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ALA A 500 |
| Chain | Residue |
| A | MET302 |
| A | ALA306 |
| A | ARG322 |
| A | SER354 |
| A | SER355 |
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 | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:9218780, ECO:0007744|PDB:4JDW |
| Chain | Residue | Details |
| A | ASP254 | |
| A | HIS303 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Amidino-cysteine intermediate => ECO:0000269|PubMed:9148748, ECO:0000269|PubMed:9218780, ECO:0007744|PDB:4JDW |
| Chain | Residue | Details |
| A | CYS407 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9218780, ECO:0007744|PDB:4JDW |
| Chain | Residue | Details |
| A | ASP170 | |
| A | ASP305 | |
| A | ARG322 | |
| A | SER354 | |
| A | SER355 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER46 | |
| A | SER49 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS385 |
Catalytic Information from CSA
| 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 |
