5CQZ
Human cytosolic 5'-nucleotidase II in complex with 3-(3-Imidazol-1-ylphenyl)-N-(9H-purin-6-yl)benzamide
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 | 8 |
| Details | binding site for residue GOL A 601 |
| Chain | Residue |
| A | GLU378 |
| A | TRP382 |
| A | TYR434 |
| A | SER439 |
| A | PHE441 |
| A | ARG442 |
| B | HIS486 |
| B | GLU487 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | TYR475 |
| A | LEU476 |
| A | ARG478 |
| B | ASP396 |
| B | ALA400 |
| A | LYS26 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | ASP52 |
| A | MET53 |
| A | ASP54 |
| A | THR249 |
| A | ASN250 |
| A | LYS292 |
| A | MG610 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | GLY130 |
| A | PRO131 |
| A | ARG134 |
| A | LYS140 |
| B | LYS344 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | GLN377 |
| A | GLU378 |
| A | TYR434 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | PHE191 |
| A | SER193 |
| A | VAL301 |
| A | LEU302 |
| A | THR316 |
| A | THR318 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 607 |
| Chain | Residue |
| A | ASP289 |
| A | GLY310 |
| A | LEU312 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 608 |
| Chain | Residue |
| A | THR147 |
| A | GLU148 |
| A | TYR151 |
| A | ARG195 |
| A | PHE198 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 609 |
| Chain | Residue |
| A | GLU487 |
| A | SER488 |
| A | VAL490 |
| B | TRP382 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 610 |
| Chain | Residue |
| A | ASP52 |
| A | ASP54 |
| A | ASP351 |
| A | SO4603 |
| A | HOH729 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue 53O A 612 |
| Chain | Residue |
| A | SER40 |
| A | ARG478 |
| B | GLN420 |
| B | SER445 |
| B | ARG446 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 601 |
| Chain | Residue |
| A | HIS486 |
| A | GLU487 |
| B | GLU378 |
| B | TRP382 |
| B | TYR434 |
| B | SER439 |
| B | PHE441 |
| B | ARG442 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 602 |
| Chain | Residue |
| A | ASP396 |
| A | ALA400 |
| B | LYS26 |
| B | TYR475 |
| B | LEU476 |
| B | ARG478 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 603 |
| Chain | Residue |
| B | ASP52 |
| B | MET53 |
| B | ASP54 |
| B | THR249 |
| B | ASN250 |
| B | LYS292 |
| B | MG607 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 604 |
| Chain | Residue |
| A | LYS344 |
| B | GLY130 |
| B | PRO131 |
| B | ARG134 |
| B | LYS140 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 605 |
| Chain | Residue |
| B | PHE157 |
| B | ARG202 |
| B | VAL205 |
| B | ASP206 |
| B | HIS209 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 606 |
| Chain | Residue |
| B | LEU483 |
| B | GLU487 |
| B | SER488 |
| B | VAL490 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 607 |
| Chain | Residue |
| B | ASP52 |
| B | ASP54 |
| B | ASP351 |
| B | SO4603 |
| B | HOH703 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue MG B 608 |
| Chain | Residue |
| B | TYR457 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue 53O B 609 |
| Chain | Residue |
| A | SER445 |
| A | ARG446 |
| B | SER40 |
| B | ARG478 |
| A | GLN420 |
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 | ASP52 | |
| B | ASP52 |
| 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 | ASP52 | |
| A | ASP54 | |
| B | ASP52 | |
| 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 |
