5AES
Crystal Structure of murine Chronophin (Pyridoxal Phosphate Phosphatase) in Complex with a PNP-derived Inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005911 | cellular_component | cell-cell junction |
| A | 0006470 | biological_process | protein dephosphorylation |
| A | 0007088 | biological_process | regulation of mitotic nuclear division |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0016020 | cellular_component | membrane |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0030027 | cellular_component | lamellipodium |
| A | 0030496 | cellular_component | midbody |
| A | 0030836 | biological_process | positive regulation of actin filament depolymerization |
| A | 0031072 | molecular_function | heat shock protein binding |
| A | 0031247 | biological_process | actin rod assembly |
| A | 0031258 | cellular_component | lamellipodium membrane |
| A | 0032154 | cellular_component | cleavage furrow |
| A | 0032361 | biological_process | pyridoxal phosphate catabolic process |
| A | 0032465 | biological_process | regulation of cytokinesis |
| A | 0032587 | cellular_component | ruffle membrane |
| A | 0033883 | molecular_function | pyridoxal phosphatase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042995 | cellular_component | cell projection |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070938 | cellular_component | contractile ring |
| A | 0071318 | biological_process | cellular response to ATP |
| A | 0098794 | cellular_component | postsynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0099159 | biological_process | regulation of modification of postsynaptic structure |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005911 | cellular_component | cell-cell junction |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0007088 | biological_process | regulation of mitotic nuclear division |
| B | 0015629 | cellular_component | actin cytoskeleton |
| B | 0016020 | cellular_component | membrane |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0030027 | cellular_component | lamellipodium |
| B | 0030496 | cellular_component | midbody |
| B | 0030836 | biological_process | positive regulation of actin filament depolymerization |
| B | 0031072 | molecular_function | heat shock protein binding |
| B | 0031247 | biological_process | actin rod assembly |
| B | 0031258 | cellular_component | lamellipodium membrane |
| B | 0032154 | cellular_component | cleavage furrow |
| B | 0032361 | biological_process | pyridoxal phosphate catabolic process |
| B | 0032465 | biological_process | regulation of cytokinesis |
| B | 0032587 | cellular_component | ruffle membrane |
| B | 0033883 | molecular_function | pyridoxal phosphatase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042995 | cellular_component | cell projection |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070938 | cellular_component | contractile ring |
| B | 0071318 | biological_process | cellular response to ATP |
| B | 0098794 | cellular_component | postsynapse |
| B | 0098978 | cellular_component | glutamatergic synapse |
| B | 0099159 | biological_process | regulation of modification of postsynaptic structure |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 305 |
| Chain | Residue |
| A | ASP25 |
| A | ASP27 |
| A | ASP234 |
| A | 5B0306 |
| A | HOH2002 |
| A | HOH2003 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 5B0 A 306 |
| Chain | Residue |
| A | SER58 |
| A | ASN59 |
| A | ASN60 |
| A | TYR146 |
| A | HIS178 |
| A | LYS209 |
| A | MG305 |
| A | HOH2002 |
| A | HOH2003 |
| A | HOH2018 |
| A | ASP25 |
| A | CYS26 |
| A | ASP27 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 305 |
| Chain | Residue |
| B | ASP25 |
| B | ASP27 |
| B | ASP234 |
| B | 5B0306 |
| B | HOH2001 |
| B | HOH2002 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5B0 B 306 |
| Chain | Residue |
| B | ASP25 |
| B | CYS26 |
| B | ASP27 |
| B | SER58 |
| B | ASN59 |
| B | ASN60 |
| B | ARG62 |
| B | TYR146 |
| B | HIS178 |
| B | LYS209 |
| B | MG305 |
| B | GOL1292 |
| B | HOH2001 |
| B | HOH2002 |
| B | HOH2003 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1292 |
| Chain | Residue |
| B | ASP27 |
| B | TRP31 |
| B | ASN60 |
| B | ARG62 |
| B | ARG63 |
| B | 5B0306 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24338687","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25783190","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4BX2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AES","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"24338687","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25783190","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4BX2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AES","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24338473","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24338687","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25783190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BKM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BX2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BX3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AES","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24338687","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25783190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BX2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AES","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25783190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AES","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
