4NZO
Crystal structure of the catalytic domain of PPIP5K2 in complex with AMPPNP and 2,5-DI-O-BN-INSP4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000829 | molecular_function | inositol heptakisphosphate kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ANP A 401 |
| Chain | Residue |
| A | ARG134 |
| A | ASP246 |
| A | LYS248 |
| A | SER264 |
| A | ASP309 |
| A | LEU311 |
| A | CYS320 |
| A | ASP321 |
| A | ASN323 |
| A | MG403 |
| A | MG404 |
| A | PRO149 |
| A | HOH568 |
| A | HOH575 |
| A | HOH665 |
| A | HOH721 |
| A | HOH804 |
| A | HOH836 |
| A | LYS187 |
| A | HIS194 |
| A | LEU211 |
| A | GLU237 |
| A | GLU238 |
| A | PHE239 |
| A | MET240 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 2OV A 402 |
| Chain | Residue |
| A | LYS53 |
| A | LYS54 |
| A | HIS101 |
| A | SER102 |
| A | LYS103 |
| A | GLU192 |
| A | ARG213 |
| A | HOH767 |
| A | HOH813 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | ASP321 |
| A | ASN323 |
| A | ANP401 |
| A | HOH721 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 404 |
| Chain | Residue |
| A | ASP309 |
| A | ASP321 |
| A | ANP401 |
| A | HOH665 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 405 |
| Chain | Residue |
| A | SER68 |
| A | PHE70 |
| A | ILE73 |
| A | HOH645 |
| A | HOH756 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22119861, ECO:0007744|PDB:3T9C, ECO:0007744|PDB:3T9D, ECO:0007744|PDB:3T9E, ECO:0007744|PDB:3T9F |
| Chain | Residue | Details |
| A | LYS248 | |
| A | LYS53 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22119861, ECO:0007744|PDB:3T54, ECO:0007744|PDB:3T7A, ECO:0007744|PDB:3T99, ECO:0007744|PDB:3T9A, ECO:0007744|PDB:3T9B, ECO:0007744|PDB:3T9C, ECO:0007744|PDB:3T9D, ECO:0007744|PDB:3T9E, ECO:0007744|PDB:3T9F |
| Chain | Residue | Details |
| A | LYS187 | |
| A | HIS194 | |
| A | GLU237 | |
| A | ARG134 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22119861, ECO:0007744|PDB:3T9A, ECO:0007744|PDB:3T9B, ECO:0007744|PDB:3T9C, ECO:0007744|PDB:3T9D |
| Chain | Residue | Details |
| A | ARG213 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22119861, ECO:0007744|PDB:3T54, ECO:0007744|PDB:3T9A, ECO:0007744|PDB:3T9B, ECO:0007744|PDB:3T9C, ECO:0007744|PDB:3T9D |
| Chain | Residue | Details |
| A | ASP246 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22119861, ECO:0007744|PDB:3T9C, ECO:0007744|PDB:3T9E, ECO:0007744|PDB:3T9F |
| Chain | Residue | Details |
| A | ARG262 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22119861, ECO:0007744|PDB:3T54, ECO:0007744|PDB:3T7A |
| Chain | Residue | Details |
| A | SER264 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22119861, ECO:0007744|PDB:3T54, ECO:0007744|PDB:3T7A, ECO:0007744|PDB:3T99, ECO:0007744|PDB:3T9B, ECO:0007744|PDB:3T9C, ECO:0007744|PDB:3T9D, ECO:0007744|PDB:3T9E, ECO:0007744|PDB:3T9F |
| Chain | Residue | Details |
| A | ASP309 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22119861, ECO:0007744|PDB:3T54 |
| Chain | Residue | Details |
| A | ASP321 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22119861, ECO:0007744|PDB:3T9D, ECO:0007744|PDB:3T9E |
| Chain | Residue | Details |
| A | SER326 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER223 |
