2WUF
Crystal structure of S114A mutant of HsaD from Mycobacterium tuberculosis in complex with 4,9DSHA
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 | 13 |
Details | BINDING SITE FOR RESIDUE KEM B 1289 |
Chain | Residue |
B | GLY44 |
B | PHE212 |
B | HIS269 |
B | TRP270 |
B | HOH2093 |
B | GLY45 |
B | GLY46 |
B | ALA49 |
B | ASN54 |
B | ALA114 |
B | LEU115 |
B | LEU158 |
B | ARG192 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1289 |
Chain | Residue |
A | PHE9 |
A | TRP52 |
A | HOH2089 |
A | HOH2090 |
B | ARG167 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL B 1290 |
Chain | Residue |
B | PHE15 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SCN A 1290 |
Chain | Residue |
A | ARG130 |
B | TYR127 |
B | PRO128 |
B | ALA129 |
B | ARG130 |
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 | ALA114 | |
B | ALA114 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qj4 |
Chain | Residue | Details |
A | HIS269 | |
A | ALA114 | |
A | ASP241 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1qj4 |
Chain | Residue | Details |
B | HIS269 | |
B | ALA114 | |
B | ASP241 |