1ZZ3
Crystal structure of a HDAC-like protein with CypX 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 | 11 |
| Details | BINDING SITE FOR RESIDUE 3YP A 1452 |
| Chain | Residue |
| A | HIS142 |
| A | ZN1451 |
| D | PHE341 |
| A | HIS143 |
| A | GLY151 |
| A | PHE152 |
| A | ASP180 |
| A | HIS182 |
| A | PHE208 |
| A | ASP268 |
| A | TYR312 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 3YP B 1552 |
| Chain | Residue |
| B | ILE100 |
| B | HIS142 |
| B | HIS143 |
| B | GLY151 |
| B | PHE152 |
| B | ASP180 |
| B | HIS182 |
| B | PHE208 |
| B | ASP268 |
| B | GLY310 |
| B | TYR312 |
| B | ZN1551 |
| C | PHE341 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 3YP C 1652 |
| Chain | Residue |
| C | ILE100 |
| C | HIS142 |
| C | HIS143 |
| C | GLY151 |
| C | PHE152 |
| C | ASP180 |
| C | HIS182 |
| C | PHE208 |
| C | ASP268 |
| C | GLY310 |
| C | TYR312 |
| C | ZN1651 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 3YP D 1752 |
| Chain | Residue |
| D | ILE100 |
| D | HIS142 |
| D | HIS143 |
| D | GLY151 |
| D | PHE152 |
| D | ASP180 |
| D | HIS182 |
| D | PHE208 |
| D | ASP268 |
| D | TYR312 |
| D | ZN1751 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1451 |
| Chain | Residue |
| A | ASP180 |
| A | HIS182 |
| A | ASP268 |
| A | 3YP1452 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1551 |
| Chain | Residue |
| B | ASP180 |
| B | HIS182 |
| B | ASP268 |
| B | 3YP1552 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1651 |
| Chain | Residue |
| C | ASP180 |
| C | HIS182 |
| C | ASP268 |
| C | 3YP1652 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1751 |
| Chain | Residue |
| D | ASP180 |
| D | HIS182 |
| D | ASP268 |
| D | 3YP1752 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1450 |
| Chain | Residue |
| A | ASP178 |
| A | ASP180 |
| A | HIS182 |
| A | SER201 |
| A | LEU202 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1550 |
| Chain | Residue |
| B | ASP178 |
| B | ASP180 |
| B | HIS182 |
| B | SER201 |
| B | LEU202 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 1650 |
| Chain | Residue |
| C | ASP178 |
| C | ASP180 |
| C | HIS182 |
| C | SER201 |
| C | LEU202 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 1750 |
| Chain | Residue |
| D | ASP178 |
| D | ASP180 |
| D | HIS182 |
| D | SER201 |
| D | LEU202 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 1449 |
| Chain | Residue |
| A | TRP191 |
| A | ASP194 |
| A | VAL197 |
| A | TYR226 |
| A | HOH1518 |
| A | HOH1581 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 1549 |
| Chain | Residue |
| B | TRP191 |
| B | ASP194 |
| B | VAL197 |
| B | TYR226 |
| B | HOH1633 |
| B | HOH1679 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 1649 |
| Chain | Residue |
| C | HOH1744 |
| C | HOH1754 |
| C | TRP191 |
| C | ASP194 |
| C | VAL197 |
| C | TYR226 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 1749 |
| Chain | Residue |
| D | TRP191 |
| D | ASP194 |
| D | VAL197 |
| D | TYR226 |
| D | HOH1791 |
| D | HOH1801 |
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 |
