3KHP
Crystal structure of a possible dehydrogenase from Mycobacterium tuberculosis at 2.3A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
A | 0004300 | molecular_function | enoyl-CoA hydratase activity |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0016829 | molecular_function | lyase activity |
A | 0044594 | molecular_function | 17-beta-hydroxysteroid dehydrogenase (NAD+) activity |
B | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
B | 0004300 | molecular_function | enoyl-CoA hydratase activity |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0016829 | molecular_function | lyase activity |
B | 0044594 | molecular_function | 17-beta-hydroxysteroid dehydrogenase (NAD+) activity |
C | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
C | 0004300 | molecular_function | enoyl-CoA hydratase activity |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0006635 | biological_process | fatty acid beta-oxidation |
C | 0016829 | molecular_function | lyase activity |
C | 0044594 | molecular_function | 17-beta-hydroxysteroid dehydrogenase (NAD+) activity |
D | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
D | 0004300 | molecular_function | enoyl-CoA hydratase activity |
D | 0006631 | biological_process | fatty acid metabolic process |
D | 0006635 | biological_process | fatty acid beta-oxidation |
D | 0016829 | molecular_function | lyase activity |
D | 0044594 | molecular_function | 17-beta-hydroxysteroid dehydrogenase (NAD+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 301 |
Chain | Residue |
A | LEU183 |
A | GLY185 |
A | ARG187 |
A | HOH389 |
C | ARG22 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 302 |
Chain | Residue |
A | GLY34 |
A | GLY36 |
D | GLN199 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TLA B 300 |
Chain | Residue |
B | ALA77 |
B | ASP186 |
B | ASN188 |
B | HIS191 |
B | HIS209 |
B | GLY210 |
B | LEU211 |
B | HOH297 |
B | HOH507 |
B | ALA76 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 301 |
Chain | Residue |
B | LEU183 |
B | GLY185 |
B | ARG187 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 302 |
Chain | Residue |
B | GLY34 |
B | GLY36 |
C | GLN199 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL C 301 |
Chain | Residue |
A | ARG22 |
A | HOH440 |
C | LEU183 |
C | ARG187 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL D 301 |
Chain | Residue |
B | ARG22 |
D | LEU183 |
D | GLY185 |
D | ARG187 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL D 303 |
Chain | Residue |
D | HIS191 |
D | GLY210 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1s9c |
Chain | Residue | Details |
A | ILE207 | |
A | ASP186 | |
A | HIS191 | |
A | GLY210 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1s9c |
Chain | Residue | Details |
B | ILE207 | |
B | ASP186 | |
B | HIS191 | |
B | GLY210 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1s9c |
Chain | Residue | Details |
C | ILE207 | |
C | ASP186 | |
C | HIS191 | |
C | GLY210 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1s9c |
Chain | Residue | Details |
D | ILE207 | |
D | ASP186 | |
D | HIS191 | |
D | GLY210 |