4KNW
The crystal structure of human HDHD4 IN COMPLEX WITH MAGNESIUM AND THE PHOSPHATE MIMETIC VANADATE
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 | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
| B | 0005829 | cellular_component | cytosol |
| B | 0006045 | biological_process | N-acetylglucosamine biosynthetic process |
| B | 0006054 | biological_process | N-acetylneuraminate metabolic process |
| B | 0006055 | biological_process | CMP-N-acetylneuraminate biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046380 | biological_process | N-acetylneuraminate biosynthetic process |
| B | 0050124 | molecular_function | N-acylneuraminate-9-phosphatase activity |
| B | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
| C | 0005829 | cellular_component | cytosol |
| C | 0006045 | biological_process | N-acetylglucosamine biosynthetic process |
| C | 0006054 | biological_process | N-acetylneuraminate metabolic process |
| C | 0006055 | biological_process | CMP-N-acetylneuraminate biosynthetic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046380 | biological_process | N-acetylneuraminate biosynthetic process |
| C | 0050124 | molecular_function | N-acylneuraminate-9-phosphatase activity |
| C | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE VO4 A 301 |
| Chain | Residue |
| A | ASP14 |
| A | LEU15 |
| A | ASP16 |
| A | THR133 |
| A | ASN134 |
| A | LYS166 |
| A | MG302 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | ASP191 |
| A | VO4301 |
| A | ASP14 |
| A | ASP16 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE VO4 B 301 |
| Chain | Residue |
| B | ASP14 |
| B | LEU15 |
| B | ASP16 |
| B | THR133 |
| B | ASN134 |
| B | LYS166 |
| B | ASP196 |
| B | MG302 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | ASP14 |
| B | ASP16 |
| B | ASP191 |
| B | THR192 |
| B | VO4301 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE VO4 C 301 |
| Chain | Residue |
| C | ASP14 |
| C | LEU15 |
| C | ASP16 |
| C | THR133 |
| C | ASN134 |
| C | LYS166 |
| C | ASP196 |
| C | MG302 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 302 |
| Chain | Residue |
| C | ASP14 |
| C | ASP16 |
| C | ASP191 |
| C | VO4301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| 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 | 3 |
| 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 | 12 |
| 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 |






