2GH6
Crystal structure of a HDAC-like protein with 9,9,9-trifluoro-8-oxo-N-phenylnonan amide bound
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
A | 0004407 | molecular_function | histone deacetylase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006338 | biological_process | chromatin remodeling |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
B | 0004407 | molecular_function | histone deacetylase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006338 | biological_process | chromatin remodeling |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
C | 0004407 | molecular_function | histone deacetylase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006338 | biological_process | chromatin remodeling |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
D | 0004407 | molecular_function | histone deacetylase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006338 | biological_process | chromatin remodeling |
D | 0016787 | molecular_function | hydrolase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 9451 |
Chain | Residue |
A | ASP180 |
A | HIS182 |
A | ASP268 |
A | CF39452 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 9551 |
Chain | Residue |
B | ASP180 |
B | HIS182 |
B | ASP268 |
B | CF39552 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 9651 |
Chain | Residue |
C | HIS182 |
C | ASP268 |
C | CF39652 |
C | ASP180 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 9751 |
Chain | Residue |
D | ASP180 |
D | HIS182 |
D | ASP268 |
D | CF39752 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 9450 |
Chain | Residue |
A | ASP178 |
A | ASP180 |
A | HIS182 |
A | SER201 |
A | LEU202 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K B 9550 |
Chain | Residue |
B | ASP178 |
B | ASP180 |
B | HIS182 |
B | SER201 |
B | LEU202 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K C 9650 |
Chain | Residue |
C | ASP178 |
C | ASP180 |
C | HIS182 |
C | SER201 |
C | LEU202 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K D 9750 |
Chain | Residue |
D | ASP178 |
D | ASP180 |
D | HIS182 |
D | SER201 |
D | LEU202 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 9449 |
Chain | Residue |
A | TRP191 |
A | ASP194 |
A | VAL197 |
A | TYR226 |
A | HOH9476 |
A | HOH9574 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K B 9549 |
Chain | Residue |
B | TRP191 |
B | ASP194 |
B | VAL197 |
B | TYR226 |
B | HOH9643 |
B | HOH9759 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K C 9649 |
Chain | Residue |
C | TRP191 |
C | ASP194 |
C | VAL197 |
C | TYR226 |
C | HOH9715 |
C | HOH9724 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K D 9749 |
Chain | Residue |
D | TRP191 |
D | ASP194 |
D | VAL197 |
D | TYR226 |
D | HOH9849 |
site_id | BC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE CF3 A 9452 |
Chain | Residue |
A | LEU21 |
A | ILE100 |
A | PRO140 |
A | HIS142 |
A | HIS143 |
A | GLY151 |
A | PHE152 |
A | CYS153 |
A | ASP180 |
A | HIS182 |
A | PHE208 |
A | ASP268 |
A | GLU309 |
A | GLY310 |
A | TYR312 |
A | ZN9451 |
A | HOH9535 |
B | PHE341 |
site_id | BC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE CF3 B 9552 |
Chain | Residue |
A | PHE341 |
B | LEU21 |
B | ILE100 |
B | PRO140 |
B | HIS142 |
B | HIS143 |
B | GLY151 |
B | PHE152 |
B | CYS153 |
B | ASP180 |
B | HIS182 |
B | PHE208 |
B | ASP268 |
B | GLU309 |
B | GLY310 |
B | TYR312 |
B | ZN9551 |
B | HOH9570 |
site_id | BC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE CF3 C 9652 |
Chain | Residue |
C | HIS143 |
C | GLY151 |
C | PHE152 |
C | CYS153 |
C | ASP180 |
C | HIS182 |
C | PHE208 |
C | ASP268 |
C | GLU309 |
C | GLY310 |
C | TYR312 |
C | ZN9651 |
C | HOH9677 |
C | HOH9820 |
D | PHE341 |
C | LEU21 |
C | ILE100 |
C | PRO140 |
C | HIS142 |
site_id | BC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE CF3 D 9752 |
Chain | Residue |
C | PHE341 |
D | LEU21 |
D | ILE100 |
D | PRO140 |
D | HIS142 |
D | HIS143 |
D | GLY151 |
D | PHE152 |
D | CYS153 |
D | ASP180 |
D | HIS182 |
D | PHE208 |
D | ASP268 |
D | GLU309 |
D | GLY310 |
D | TYR312 |
D | ZN9751 |
D | HOH9785 |
D | HOH9828 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q48935 |
Chain | Residue | Details |
A | ALA144 | |
B | ALA144 | |
C | ALA144 | |
D | ALA144 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27756124, ECO:0007744|PDB:5G1C |
Chain | Residue | Details |
A | VAL181 | |
D | VAL181 | |
D | HIS183 | |
D | ALA269 | |
A | HIS183 | |
A | ALA269 | |
B | VAL181 | |
B | HIS183 | |
B | ALA269 | |
C | VAL181 | |
C | HIS183 | |
C | ALA269 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Polarizes the scissile carbonyl of the substrate => ECO:0000250|UniProtKB:Q48935 |
Chain | Residue | Details |
A | SER313 | |
B | SER313 | |
C | SER313 | |
D | SER313 |