6DDQ
Crystal structure of the double mutant (R39Q/D52N) of the full-length NT5C2 in the basal state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000255 | biological_process | allantoin metabolic process |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006204 | biological_process | IMP catabolic process |
A | 0008253 | molecular_function | 5'-nucleotidase activity |
A | 0009117 | biological_process | nucleotide metabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0046037 | biological_process | GMP metabolic process |
A | 0046040 | biological_process | IMP metabolic process |
A | 0046054 | biological_process | dGMP metabolic process |
A | 0046085 | biological_process | adenosine metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0050146 | molecular_function | nucleoside phosphotransferase activity |
A | 0050483 | molecular_function | IMP 5'-nucleotidase activity |
A | 0050484 | molecular_function | GMP 5'-nucleotidase activity |
A | 0050689 | biological_process | negative regulation of defense response to virus by host |
A | 0061630 | molecular_function | ubiquitin protein ligase activity |
A | 0070936 | biological_process | protein K48-linked ubiquitination |
A | 0106411 | molecular_function | XMP 5'-nucleosidase activity |
B | 0000255 | biological_process | allantoin metabolic process |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006204 | biological_process | IMP catabolic process |
B | 0008253 | molecular_function | 5'-nucleotidase activity |
B | 0009117 | biological_process | nucleotide metabolic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0046037 | biological_process | GMP metabolic process |
B | 0046040 | biological_process | IMP metabolic process |
B | 0046054 | biological_process | dGMP metabolic process |
B | 0046085 | biological_process | adenosine metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0050146 | molecular_function | nucleoside phosphotransferase activity |
B | 0050483 | molecular_function | IMP 5'-nucleotidase activity |
B | 0050484 | molecular_function | GMP 5'-nucleotidase activity |
B | 0050689 | biological_process | negative regulation of defense response to virus by host |
B | 0061630 | molecular_function | ubiquitin protein ligase activity |
B | 0070936 | biological_process | protein K48-linked ubiquitination |
B | 0106411 | molecular_function | XMP 5'-nucleosidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue PO4 A 601 |
Chain | Residue |
A | ARG34 |
A | HOH904 |
A | HOH964 |
A | VAL35 |
A | VAL37 |
A | TYR471 |
A | TYR475 |
A | PHE477 |
A | HOH725 |
A | HOH728 |
A | HOH734 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue PO4 A 602 |
Chain | Residue |
A | ASN52 |
A | MET53 |
A | ASP54 |
A | THR249 |
A | ASN250 |
A | LYS292 |
A | HOH776 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 603 |
Chain | Residue |
A | MET430 |
A | ASP431 |
A | ARG442 |
A | GLY444 |
A | HIS546 |
A | HOH722 |
A | HOH731 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue PO4 B 601 |
Chain | Residue |
B | ARG34 |
B | VAL35 |
B | VAL37 |
B | TYR471 |
B | TYR475 |
B | PHE477 |
B | HOH760 |
B | HOH763 |
B | HOH812 |
B | HOH840 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue PO4 B 602 |
Chain | Residue |
B | ASN52 |
B | MET53 |
B | ASP54 |
B | THR249 |
B | ASN250 |
B | SER251 |
B | LYS292 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO B 603 |
Chain | Residue |
B | ASP252 |
B | TYR253 |
B | VAL288 |
B | ASP289 |
B | LEU312 |
B | HOH880 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:21396942 |
Chain | Residue | Details |
A | ASN52 | |
B | ASN52 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:21396942 |
Chain | Residue | Details |
A | ASP54 | |
B | ASP54 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2J2C, ECO:0007744|PDB:2JC9, ECO:0007744|PDB:2JCM, ECO:0007744|PDB:2XCV, ECO:0007744|PDB:2XCW, ECO:0007744|PDB:2XJB, ECO:0007744|PDB:2XJC, ECO:0007744|PDB:2XJD, ECO:0007744|PDB:2XJE |
Chain | Residue | Details |
A | ASN52 | |
A | ASP54 | |
B | ASN52 | |
B | ASP54 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XJB |
Chain | Residue | Details |
A | ARG144 | |
A | ARG456 | |
B | ARG144 | |
B | ARG456 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XJC |
Chain | Residue | Details |
A | ASN154 | |
A | LYS362 | |
A | GLN453 | |
A | TYR457 | |
B | ASN154 | |
B | LYS362 | |
B | GLN453 | |
B | TYR457 |
site_id | SWS_FT_FI6 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XCV, ECO:0007744|PDB:2XCW |
Chain | Residue | Details |
A | ARG202 | |
B | LYS215 | |
B | THR249 | |
B | ASN250 | |
B | SER251 | |
B | LYS292 | |
A | ASP206 | |
A | LYS215 | |
A | THR249 | |
A | ASN250 | |
A | SER251 | |
A | LYS292 | |
B | ARG202 | |
B | ASP206 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2J2C, ECO:0007744|PDB:2JC9, ECO:0007744|PDB:2JCM |
Chain | Residue | Details |
A | ASP351 | |
B | ASP351 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0007744|PDB:2JC9 |
Chain | Residue | Details |
A | MET436 | |
B | MET436 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER418 | |
A | SER511 | |
B | SER418 | |
B | SER511 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER502 | |
B | SER502 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3V1L4 |
Chain | Residue | Details |
A | SER527 | |
B | SER527 |