2VF2
X-ray crystal structure of HsaD from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018774 | molecular_function | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity |
| A | 0034820 | molecular_function | 4,9-DSHA hydrolase activity |
| A | 0051701 | biological_process | biological process involved in interaction with host |
| A | 0102296 | molecular_function | 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006694 | biological_process | steroid biosynthetic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018774 | molecular_function | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity |
| B | 0034820 | molecular_function | 4,9-DSHA hydrolase activity |
| B | 0051701 | biological_process | biological process involved in interaction with host |
| B | 0102296 | molecular_function | 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B1291 |
| Chain | Residue |
| B | SER143 |
| B | ILE144 |
| B | ASN145 |
| B | ASP150 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A1291 |
| Chain | Residue |
| A | THR53 |
| A | SER56 |
| A | PRO186 |
| A | GLU187 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B1292 |
| Chain | Residue |
| B | HIS85 |
| B | GLY86 |
| B | TYR91 |
| B | MET94 |
| B | HOH2077 |
| B | HOH2078 |
| B | ASP21 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A1292 |
| Chain | Residue |
| A | ARG157 |
| A | ARG175 |
| A | LYS181 |
| A | HOH2126 |
| B | LYS156 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B1293 |
| Chain | Residue |
| A | LYS156 |
| B | ARG157 |
| B | LYS181 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS269 | |
| B | HIS269 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY45 | |
| A | ASN54 | |
| A | LEU115 | |
| B | GLY45 | |
| B | ASN54 | |
| B | LEU115 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN113 | |
| A | ARG192 | |
| A | TRP270 | |
| B | ASN113 | |
| B | ARG192 | |
| B | TRP270 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | SER114 | |
| B | SER114 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azw |
| Chain | Residue | Details |
| A | HIS269 | |
| A | SER114 | |
| A | ASP241 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azw |
| Chain | Residue | Details |
| B | HIS269 | |
| B | SER114 | |
| B | ASP241 |
