2XJF
Crystal structure of the D52N variant of cytosolic 5'-nucleotidase II with a covalently modified Asn52
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE DG2 A 1489 |
Chain | Residue |
A | ARG144 |
A | TYR457 |
A | ARG144 |
A | LYS362 |
A | LYS362 |
A | GLN453 |
A | GLN453 |
A | ARG456 |
A | ARG456 |
A | TYR457 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 1490 |
Chain | Residue |
A | PHE283 |
A | ASP284 |
A | LEU285 |
A | ILE286 |
A | GLN322 |
A | HIS323 |
A | GLY324 |
A | ILE325 |
A | HOH2250 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1491 |
Chain | Residue |
A | PHE157 |
A | ARG202 |
A | VAL205 |
A | ASP206 |
A | TYR210 |
A | HOH2103 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1492 |
Chain | Residue |
A | ASP252 |
A | TYR253 |
A | VAL288 |
A | ASP289 |
A | GLY310 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:21396942 |
Chain | Residue | Details |
A | A5N52 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:21396942 |
Chain | Residue | Details |
A | ASP54 |
site_id | SWS_FT_FI3 |
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, 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 | A5N52 | |
A | ASP54 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XJB |
Chain | Residue | Details |
A | ARG144 | |
A | ARG456 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XJC |
Chain | Residue | Details |
A | ASN154 | |
A | LYS362 | |
A | GLN453 | |
A | TYR457 |
site_id | SWS_FT_FI6 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21396942, ECO:0007744|PDB:2XCV, ECO:0007744|PDB:2XCW |
Chain | Residue | Details |
A | ARG202 | |
A | ASP206 | |
A | LYS215 | |
A | THR249 | |
A | ASN250 | |
A | SER251 | |
A | LYS292 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
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 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17405878, ECO:0007744|PDB:2JC9 |
Chain | Residue | Details |
A | MET436 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER418 | |
A | SER511 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER502 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3V1L4 |
Chain | Residue | Details |
A | SER527 |