5OPL
Crystal structure of K25E cN-II mutant
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 | 4 |
| Details | binding site for residue GOL A 601 |
| Chain | Residue |
| A | LEU41 |
| A | ALA42 |
| A | LYS45 |
| A | ARG367 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | ILE325 |
| A | HOH715 |
| A | HOH720 |
| A | HOH730 |
| A | ASP284 |
| A | LEU321 |
| A | GLN322 |
| A | HIS323 |
| A | GLY324 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | ARG144 |
| A | LYS362 |
| A | LYS362 |
| A | GLN453 |
| A | TYR457 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 604 |
| Chain | Residue |
| A | PRO96 |
| A | THR97 |
| A | GLU378 |
| A | TYR434 |
| A | GLY438 |
| A | HOH702 |
| A | HOH779 |
| A | HOH791 |
| A | HOH835 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 605 |
| Chain | Residue |
| A | PHE157 |
| A | ARG202 |
| A | VAL205 |
| A | ASP206 |
| A | TYR210 |
| A | HOH745 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 606 |
| Chain | Residue |
| A | ASP54 |
| A | TYR65 |
| A | HIS209 |
| A | LYS215 |
| A | SER251 |
| A | TYR255 |
| A | HOH705 |
| A | HOH711 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 607 |
| Chain | Residue |
| A | ASN154 |
| A | HIS352 |
| A | HOH726 |
| A | HOH797 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 608 |
| Chain | Residue |
| A | PHE172 |
| A | THR173 |
| A | CYS175 |
| A | PRO176 |
| A | TYR178 |
| A | THR179 |
| A | SER180 |
| A | HOH839 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 609 |
| Chain | Residue |
| A | TYR151 |
| A | GLN199 |
| A | ARG202 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 610 |
| Chain | Residue |
| A | ASP52 |
| A | ASP54 |
| A | ASP351 |
| A | HIS352 |
| A | HOH736 |
| A | HOH770 |
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 | ASP52 |
| 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 | ASP52 | |
| 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 |
