6GIU
Human IMPase with L-690330
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004346 | molecular_function | glucose-6-phosphatase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006020 | biological_process | inositol metabolic process |
| A | 0006021 | biological_process | inositol biosynthetic process |
| A | 0006661 | biological_process | phosphatidylinositol biosynthetic process |
| A | 0006796 | biological_process | phosphate-containing compound metabolic process |
| A | 0007165 | biological_process | signal transduction |
| A | 0008877 | molecular_function | glucose-1-phosphatase activity |
| A | 0008934 | molecular_function | inositol monophosphate 1-phosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0031403 | molecular_function | lithium ion binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047954 | molecular_function | glycerol-2-phosphatase activity |
| A | 0052832 | molecular_function | inositol monophosphate 3-phosphatase activity |
| A | 0052833 | molecular_function | inositol monophosphate 4-phosphatase activity |
| A | 0052834 | molecular_function | inositol monophosphate phosphatase activity |
| A | 0103026 | molecular_function | fructose-1-phosphatase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004346 | molecular_function | glucose-6-phosphatase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006020 | biological_process | inositol metabolic process |
| B | 0006021 | biological_process | inositol biosynthetic process |
| B | 0006661 | biological_process | phosphatidylinositol biosynthetic process |
| B | 0006796 | biological_process | phosphate-containing compound metabolic process |
| B | 0007165 | biological_process | signal transduction |
| B | 0008877 | molecular_function | glucose-1-phosphatase activity |
| B | 0008934 | molecular_function | inositol monophosphate 1-phosphatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0031403 | molecular_function | lithium ion binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047954 | molecular_function | glycerol-2-phosphatase activity |
| B | 0052832 | molecular_function | inositol monophosphate 3-phosphatase activity |
| B | 0052833 | molecular_function | inositol monophosphate 4-phosphatase activity |
| B | 0052834 | molecular_function | inositol monophosphate phosphatase activity |
| B | 0103026 | molecular_function | fructose-1-phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 301 |
| Chain | Residue |
| A | GLU70 |
| A | L69304 |
| A | HOH466 |
| A | HOH524 |
| A | HOH541 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 302 |
| Chain | Residue |
| A | L69304 |
| A | HOH425 |
| A | GLU70 |
| A | ASP90 |
| A | ILE92 |
| A | MN303 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 303 |
| Chain | Residue |
| A | ASP90 |
| A | ASP93 |
| A | ASP220 |
| A | MN302 |
| A | L69304 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue L69 A 304 |
| Chain | Residue |
| A | GLU70 |
| A | ASP90 |
| A | ILE92 |
| A | ASP93 |
| A | GLY94 |
| A | THR95 |
| A | GLU162 |
| A | GLY194 |
| A | THR195 |
| A | ALA196 |
| A | GLU213 |
| A | HIS217 |
| A | TRP219 |
| A | ASP220 |
| A | MN301 |
| A | MN302 |
| A | MN303 |
| A | GOL305 |
| A | GOL306 |
| A | GOL313 |
| A | HOH440 |
| A | HOH466 |
| A | HOH524 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 305 |
| Chain | Residue |
| A | GLY164 |
| A | SER165 |
| A | GLU213 |
| A | GLY215 |
| A | L69304 |
| A | GOL306 |
| A | GOL309 |
| A | GOL313 |
| A | HOH419 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 306 |
| Chain | Residue |
| A | THR96 |
| A | GLU162 |
| A | GLY164 |
| A | L69304 |
| A | GOL305 |
| A | HOH440 |
| A | HOH484 |
| A | HOH489 |
| B | ARG191 |
| B | HOH405 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 307 |
| Chain | Residue |
| A | ARG191 |
| A | HOH410 |
| A | HOH444 |
| A | HOH494 |
| B | THR96 |
| B | GLU162 |
| B | GLY164 |
| B | GOL306 |
| B | HOH530 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 308 |
| Chain | Residue |
| A | ARG261 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 309 |
| Chain | Residue |
| A | SER165 |
| A | SER166 |
| A | GLY215 |
| A | ARG248 |
| A | GOL305 |
| A | GOL313 |
| A | GOL316 |
| A | HOH465 |
| A | HOH485 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 310 |
| Chain | Residue |
| A | LYS78 |
| A | SER79 |
| A | ASP274 |
| A | GLU276 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 311 |
| Chain | Residue |
| A | LEU163 |
| A | MET179 |
| A | ILE190 |
| A | SER192 |
| A | HOH403 |
| A | HOH406 |
| B | LEU163 |
| B | SER192 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 312 |
| Chain | Residue |
| A | LYS36 |
| A | ALA74 |
| A | HOH438 |
| A | HOH506 |
| B | LYS36 |
| B | SER38 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 313 |
| Chain | Residue |
| A | L69304 |
| A | GOL305 |
| A | GOL309 |
| A | HOH411 |
| A | SER37 |
| A | SER165 |
| A | HIS217 |
| A | ARG248 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 314 |
| Chain | Residue |
| A | SER149 |
| A | GLN151 |
| A | LYS156 |
| A | HIS188 |
| A | ASP209 |
| A | GOL315 |
| A | HOH436 |
| A | HOH577 |
| B | VAL99 |
| B | HIS100 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 315 |
| Chain | Residue |
| A | SER149 |
| A | GLN150 |
| A | GLN151 |
| A | GOL314 |
| A | HOH591 |
| A | HOH625 |
| B | ARG101 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 316 |
| Chain | Residue |
| A | ARG248 |
| A | PRO270 |
| A | LEU271 |
| A | GLN272 |
| A | GOL309 |
| A | HOH465 |
| A | HOH467 |
| A | HOH468 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 301 |
| Chain | Residue |
| B | ASP90 |
| B | ASP93 |
| B | ASP220 |
| B | MN302 |
| B | L69305 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 302 |
| Chain | Residue |
| B | GLU70 |
| B | ASP90 |
| B | ILE92 |
| B | MN301 |
| B | L69305 |
| B | HOH416 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 303 |
| Chain | Residue |
| B | GLU70 |
| B | L69305 |
| B | HOH451 |
| B | HOH466 |
| B | HOH541 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 304 |
| Chain | Residue |
| B | HOH433 |
| B | HOH443 |
| B | HOH465 |
| B | HOH648 |
| B | HOH668 |
| B | HOH727 |
| site_id | AE3 |
| Number of Residues | 22 |
| Details | binding site for residue L69 B 305 |
| Chain | Residue |
| A | HOH444 |
| B | GLU70 |
| B | ASP90 |
| B | ILE92 |
| B | ASP93 |
| B | GLY94 |
| B | THR95 |
| B | GLU162 |
| B | GLY194 |
| B | THR195 |
| B | ALA196 |
| B | GLU213 |
| B | HIS217 |
| B | TRP219 |
| B | ASP220 |
| B | MN301 |
| B | MN302 |
| B | MN303 |
| B | GOL306 |
| B | GOL312 |
| B | HOH451 |
| B | HOH466 |
| site_id | AE4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 306 |
| Chain | Residue |
| A | GOL307 |
| B | GLY164 |
| B | SER165 |
| B | GLU213 |
| B | GLY215 |
| B | L69305 |
| B | GOL309 |
| B | GOL312 |
| B | HOH409 |
| site_id | AE5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 307 |
| Chain | Residue |
| B | GLU30 |
| B | MET31 |
| B | ASN32 |
| B | ASP153 |
| B | THR155 |
| B | HOH439 |
| B | HOH467 |
| B | HOH513 |
| site_id | AE6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 308 |
| Chain | Residue |
| A | VAL99 |
| A | HIS100 |
| A | HOH504 |
| B | GLN151 |
| B | LYS156 |
| B | HIS188 |
| B | HOH421 |
| B | HOH440 |
| B | HOH485 |
| B | HOH521 |
| site_id | AE7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 309 |
| Chain | Residue |
| B | SER165 |
| B | SER166 |
| B | GLY215 |
| B | ARG248 |
| B | GOL306 |
| B | GOL312 |
| B | HOH457 |
| B | HOH471 |
| B | HOH480 |
| site_id | AE8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 310 |
| Chain | Residue |
| B | SER38 |
| B | VAL40 |
| B | SER165 |
| B | SER166 |
| B | ARG167 |
| B | THR168 |
| B | HOH449 |
| site_id | AE9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 311 |
| Chain | Residue |
| B | PHE140 |
| B | HOH464 |
| B | HOH604 |
| site_id | AF1 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 312 |
| Chain | Residue |
| B | SER37 |
| B | SER165 |
| B | HIS217 |
| B | ARG248 |
| B | L69305 |
| B | GOL306 |
| B | GOL309 |
| B | HOH412 |
| B | HOH471 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8068620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8068621","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23027737","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8068621","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23027737","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8068621","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1332026","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"8068620","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8068620","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 577 |
| Chain | Residue | Details |
| A | GLU70 | metal ligand, proton acceptor, proton donor |
| A | ASP90 | metal ligand |
| A | ILE92 | metal ligand |
| A | ASP93 | metal ligand |
| A | THR95 | hydrogen bond acceptor |
| A | ASP220 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 577 |
| Chain | Residue | Details |
| B | GLU70 | metal ligand, proton acceptor, proton donor |
| B | ASP90 | metal ligand |
| B | ILE92 | metal ligand |
| B | ASP93 | metal ligand |
| B | THR95 | hydrogen bond acceptor |
| B | ASP220 | metal ligand |
