2HW4
Crystal structure of human phosphohistidine phosphatase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0016604 | cellular_component | nuclear body |
| A | 0019855 | molecular_function | calcium channel inhibitor activity |
| A | 0030036 | biological_process | actin cytoskeleton organization |
| A | 0035971 | biological_process | peptidyl-histidine dephosphorylation |
| A | 0044325 | molecular_function | transmembrane transporter binding |
| A | 0050860 | biological_process | negative regulation of T cell receptor signaling pathway |
| A | 0051015 | molecular_function | actin filament binding |
| A | 0051350 | biological_process | negative regulation of lyase activity |
| A | 0061851 | cellular_component | leading edge of lamellipodium |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097581 | biological_process | lamellipodium organization |
| A | 0101006 | molecular_function | protein histidine phosphatase activity |
| A | 2000147 | biological_process | positive regulation of cell motility |
| A | 2000984 | biological_process | negative regulation of ATP citrate synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 1201 |
| Chain | Residue |
| A | HIS53 |
| A | ARG78 |
| A | SER94 |
| A | MET95 |
| A | FMT1213 |
| A | HOH1252 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 1202 |
| Chain | Residue |
| A | ARG78 |
| A | TYR91 |
| A | ALA96 |
| A | HOH1252 |
| A | TYR52 |
| A | HIS53 |
| A | ALA54 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 1203 |
| Chain | Residue |
| A | PRO10 |
| A | ASP11 |
| A | VAL12 |
| A | LYS112 |
| A | HOH1232 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 1204 |
| Chain | Residue |
| A | TYR57 |
| A | GLU72 |
| A | CYS73 |
| A | HOH1265 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 1205 |
| Chain | Residue |
| A | ASP17 |
| A | GLY18 |
| A | HIS81 |
| A | GLN82 |
| A | HOH1237 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 1206 |
| Chain | Residue |
| A | ARG45 |
| A | MET64 |
| A | HOH1234 |
| A | HOH1264 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 1207 |
| Chain | Residue |
| A | LYS21 |
| A | TYR52 |
| A | ARG78 |
| A | FMT1212 |
| A | FMT1213 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 1208 |
| Chain | Residue |
| A | ASP5 |
| A | GLU107 |
| A | ALA111 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 1209 |
| Chain | Residue |
| A | ASP15 |
| A | SER16 |
| A | FMT1214 |
| A | HOH1258 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 1210 |
| Chain | Residue |
| A | ASN122 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 1211 |
| Chain | Residue |
| A | HIS28 |
| A | ASP70 |
| A | CYS71 |
| A | GLU72 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 1212 |
| Chain | Residue |
| A | VAL19 |
| A | LYS48 |
| A | TYR52 |
| A | FMT1207 |
| A | HOH1219 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 1213 |
| Chain | Residue |
| A | LYS21 |
| A | HIS53 |
| A | ARG78 |
| A | MET95 |
| A | FMT1201 |
| A | FMT1207 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 1214 |
| Chain | Residue |
| A | TYR0 |
| A | SER16 |
| A | ASP17 |
| A | TRP120 |
| A | FMT1209 |
| A | HOH1258 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 1215 |
| Chain | Residue |
| A | GLU39 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 1216 |
| Chain | Residue |
| A | ASP13 |
| A | ILE14 |
| A | HOH1268 |
| A | HOH1271 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 1217 |
| Chain | Residue |
| A | GLU39 |
| A | SER40 |
| A | HOH1261 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:18991813 |
| Chain | Residue | Details |
| A | HIS53 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18991813 |
| Chain | Residue | Details |
| A | LYS21 | |
| A | SER94 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 952 |
| Chain | Residue | Details |
| A | LYS21 | electrostatic stabiliser, modifies pKa |
| A | HIS53 | proton acceptor, proton donor |
| A | ALA54 | electrostatic stabiliser |
| A | ARG78 | electrostatic stabiliser |
| A | SER94 | electrostatic stabiliser |
| A | ALA96 | electrostatic stabiliser |
