6GJ0
Human IMPase with Mn
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
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 | 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 | 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 |
B | 0000287 | molecular_function | magnesium ion binding |
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 | 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 | 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 |
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 | MES307 |
A | HOH429 |
A | HOH432 |
A | HOH456 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MN A 302 |
Chain | Residue |
A | HOH492 |
A | GLU70 |
A | ASP90 |
A | ILE92 |
A | MES307 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MN A 303 |
Chain | Residue |
A | ASP90 |
A | ASP93 |
A | ASP220 |
A | GOL304 |
A | MES307 |
A | HOH528 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | ASP93 |
A | THR195 |
A | ALA196 |
A | GLU213 |
A | ASP220 |
A | MN303 |
A | MES307 |
A | HOH446 |
A | HOH528 |
A | HOH552 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | LEU163 |
A | SER192 |
A | HOH407 |
A | HOH411 |
B | ILE190 |
B | ARG191 |
B | SER192 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue GOL A 306 |
Chain | Residue |
A | ARG248 |
A | LEU271 |
A | GLN272 |
A | HOH557 |
site_id | AC7 |
Number of Residues | 16 |
Details | binding site for residue MES A 307 |
Chain | Residue |
A | GLU70 |
A | ASP90 |
A | ILE92 |
A | ASP93 |
A | GLY94 |
A | THR95 |
A | THR96 |
A | MN301 |
A | MN302 |
A | MN303 |
A | GOL304 |
A | HOH426 |
A | HOH489 |
A | HOH528 |
A | HOH574 |
A | HOH585 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MN B 301 |
Chain | Residue |
B | ASP90 |
B | ASP93 |
B | ASP220 |
B | GOL304 |
B | MES307 |
B | HOH517 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue MN B 302 |
Chain | Residue |
B | GLU70 |
B | ASP90 |
B | ILE92 |
B | MES307 |
B | HOH472 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue MN B 303 |
Chain | Residue |
B | GLU70 |
B | MES307 |
B | HOH428 |
B | HOH436 |
B | HOH447 |
site_id | AD2 |
Number of Residues | 11 |
Details | binding site for residue GOL B 304 |
Chain | Residue |
B | ASP93 |
B | THR195 |
B | ALA196 |
B | GLU213 |
B | ASP220 |
B | MN301 |
B | MES307 |
B | HOH413 |
B | HOH441 |
B | HOH517 |
B | HOH540 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue GOL B 305 |
Chain | Residue |
A | VAL99 |
A | HIS100 |
B | GLN151 |
B | LYS156 |
B | HIS188 |
B | ASP209 |
B | HOH534 |
B | HOH539 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue GOL B 306 |
Chain | Residue |
B | VAL73 |
B | LYS78 |
B | SER79 |
B | ASP277 |
site_id | AD5 |
Number of Residues | 19 |
Details | binding site for residue MES B 307 |
Chain | Residue |
B | THR95 |
B | THR96 |
B | ASN97 |
B | GLY194 |
B | MN301 |
B | MN302 |
B | MN303 |
B | GOL304 |
B | HOH428 |
B | HOH429 |
B | HOH496 |
B | HOH517 |
A | ARG191 |
A | HOH536 |
B | GLU70 |
B | ASP90 |
B | ILE92 |
B | ASP93 |
B | GLY94 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8068620, ECO:0000303|PubMed:8068621 |
Chain | Residue | Details |
A | GLU70 | |
A | GLU213 | |
B | GLU70 | |
B | GLU213 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23027737, ECO:0000269|PubMed:8068621 |
Chain | Residue | Details |
A | ASP90 | |
A | ASP93 | |
B | ASP90 | |
B | ASP93 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23027737, ECO:0000269|PubMed:8068621, ECO:0000303|PubMed:1332026, ECO:0000303|PubMed:8068620 |
Chain | Residue | Details |
A | ILE92 | |
B | ILE92 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8068620 |
Chain | Residue | Details |
A | GLY194 | |
A | ASP220 | |
B | GLY194 | |
B | ASP220 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR168 | |
B | THR168 |
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 |