5DGI
Crystal structure of the catalytic domain of human diphosphoinositol pentakisphosphate kinase 2 (PPIP5K2) in complex with ADP and 3,5-(PCP)2-IP4
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 | 23 |
| Details | binding site for residue ADP A 401 |
| Chain | Residue |
| A | ARG134 |
| A | MET240 |
| A | ASP246 |
| A | SER264 |
| A | PRO265 |
| A | ASP309 |
| A | LEU311 |
| A | CYS320 |
| A | ASP321 |
| A | MG403 |
| A | MG404 |
| A | PRO149 |
| A | HOH519 |
| A | HOH549 |
| A | HOH694 |
| A | HOH736 |
| A | VAL185 |
| A | LYS187 |
| A | HIS194 |
| A | LEU211 |
| A | GLU237 |
| A | GLU238 |
| A | PHE239 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue 5A2 A 402 |
| Chain | Residue |
| A | LYS53 |
| A | LYS54 |
| A | SER102 |
| A | LYS103 |
| A | ARG213 |
| A | LYS214 |
| A | TYR250 |
| A | ARG262 |
| A | ARG273 |
| A | SER326 |
| A | LYS329 |
| A | HOH506 |
| A | HOH512 |
| A | HOH522 |
| A | HOH557 |
| A | HOH578 |
| A | HOH589 |
| A | HOH665 |
| A | HOH703 |
| A | HOH710 |
| A | HOH743 |
| A | HOH747 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASP321 |
| A | ASN323 |
| A | ADP401 |
| A | HOH515 |
| A | HOH705 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | ASP309 |
| A | ASP321 |
| A | ADP401 |
| A | HOH549 |
| A | HOH742 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 405 |
| Chain | Residue |
| A | SER68 |
| A | PHE70 |
| A | ILE73 |
| A | HOH598 |
| A | HOH653 |
| A | HOH750 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ACT A 406 |
| Chain | Residue |
| A | VAL121 |
| A | ASP124 |
| A | LEU125 |
| A | ASN126 |
| A | HOH612 |
| A | HOH658 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ASN90 |
| A | TRP91 |
| A | PRO92 |
| A | PRO283 |
| A | ILE285 |
| A | HOH554 |
| A | HOH741 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue ACT A 408 |
| Chain | Residue |
| A | SER217 |
| A | ARG218 |
| A | LYS270 |
| A | LYS291 |
| A | LEU292 |
| A | HOH542 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | LYS248 |
| A | TYR250 |
| A | GLY307 |
| A | PHE308 |
| A | ASP309 |
| A | ASN323 |
| A | SER326 |
| A | HOH522 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | ARG312 |
| A | ALA313 |
| A | GLY315 |
| A | GLN316 |
| A | SER317 |
| A | HOH518 |
| A | HOH527 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 411 |
| Chain | Residue |
| A | LYS333 |
| A | TYR334 |
| A | HOH737 |
| A | GLU89 |
| A | ASN90 |
| A | TYR256 |
| A | HIS258 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 412 |
| Chain | Residue |
| A | PHE70 |
| A | HOH656 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 413 |
| Chain | Residue |
| A | PHE105 |
| A | PRO106 |
| A | LEU107 |
| A | ASP108 |
| A | HOH501 |
| A | HOH607 |
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 | LYS53 | |
| A | LYS248 |
| 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 | ARG134 | |
| A | LYS187 | |
| A | HIS194 | |
| A | GLU237 |
| 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 |
