2W4M
The Crystal Structure of human N-acetylneuraminic acid phosphatase, NANP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0006045 | biological_process | N-acetylglucosamine biosynthetic process |
A | 0006054 | biological_process | N-acetylneuraminate metabolic process |
A | 0006055 | biological_process | CMP-N-acetylneuraminate biosynthetic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046380 | biological_process | N-acetylneuraminate biosynthetic process |
A | 0050124 | molecular_function | N-acylneuraminate-9-phosphatase activity |
A | 0070085 | biological_process | glycosylation |
A | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A1245 |
Chain | Residue |
A | ASP12 |
A | ASP14 |
A | ASP189 |
A | CL1246 |
A | PO41249 |
A | HOH2075 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A1246 |
Chain | Residue |
A | HOH2088 |
A | ASN15 |
A | THR190 |
A | NA1245 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A1247 |
Chain | Residue |
A | LYS55 |
A | LYS58 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A1248 |
Chain | Residue |
A | ARG72 |
A | ARG104 |
A | LYS141 |
A | HOH2085 |
A | HOH2086 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A1249 |
Chain | Residue |
A | ASP12 |
A | LEU13 |
A | ASP14 |
A | THR131 |
A | ASN132 |
A | LYS164 |
A | NA1245 |
A | HOH2075 |
A | HOH2087 |
A | HOH2088 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23747226","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KNV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KNW","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23747226","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KNV","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23747226","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"PDB data bank","title":"The crystal structure of human N-acetylneuraminic acid phosphatase, NANP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2W4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KNV","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1lvh |
Chain | Residue | Details |
A | GLY133 | |
A | LYS164 |