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 | 0005575 | cellular_component | cellular_component |
A | 0005829 | cellular_component | cytosol |
A | 0006045 | biological_process | N-acetylglucosamine biosynthetic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016791 | molecular_function | phosphatase activity |
A | 0044283 | biological_process | small molecule biosynthetic process |
A | 0046380 | biological_process | N-acetylneuraminate biosynthetic process |
A | 0050124 | molecular_function | N-acylneuraminate-9-phosphatase activity |
B | 0005575 | cellular_component | cellular_component |
B | 0005829 | cellular_component | cytosol |
B | 0006045 | biological_process | N-acetylglucosamine biosynthetic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016791 | molecular_function | phosphatase activity |
B | 0044283 | biological_process | small molecule biosynthetic process |
B | 0046380 | biological_process | N-acetylneuraminate biosynthetic process |
B | 0050124 | molecular_function | N-acylneuraminate-9-phosphatase activity |
C | 0005575 | cellular_component | cellular_component |
C | 0005829 | cellular_component | cytosol |
C | 0006045 | biological_process | N-acetylglucosamine biosynthetic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016791 | molecular_function | phosphatase activity |
C | 0044283 | biological_process | small molecule biosynthetic process |
C | 0046380 | biological_process | N-acetylneuraminate biosynthetic process |
C | 0050124 | molecular_function | N-acylneuraminate-9-phosphatase activity |
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 | 9 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP14 | |
A | THR133 | |
A | LYS166 | |
B | ASP14 | |
B | THR133 | |
B | LYS166 | |
C | ASP14 | |
C | THR133 | |
C | LYS166 |