5LI3
Crystal structure of HDAC-like protein from P. aeruginosa in complex with a photo-switchable inhibitor.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004407 | molecular_function | histone deacetylase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0040029 | biological_process | epigenetic regulation of gene expression |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004407 | molecular_function | histone deacetylase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0040029 | biological_process | epigenetic regulation of gene expression |
| B | 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 401 |
| Chain | Residue |
| A | ASP181 |
| A | HIS183 |
| A | ASP269 |
| A | 9RB404 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue K A 402 |
| Chain | Residue |
| A | ASP179 |
| A | ASP181 |
| A | HIS183 |
| A | SER202 |
| A | LEU203 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue K A 403 |
| Chain | Residue |
| A | TYR192 |
| A | ARG195 |
| A | VAL198 |
| A | SER200 |
| A | PHE227 |
| A | HOH503 |
| A | HOH527 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue 9RB A 404 |
| Chain | Residue |
| A | THR24 |
| A | ASP101 |
| A | HIS143 |
| A | HIS144 |
| A | PHE153 |
| A | ASP181 |
| A | HIS183 |
| A | PHE209 |
| A | ASP269 |
| A | TYR313 |
| A | ZN401 |
| A | HOH510 |
| B | LEU340 |
| B | PHE343 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | ASP181 |
| B | HIS183 |
| B | ASP269 |
| B | 9RB404 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue K B 402 |
| Chain | Residue |
| B | ASP179 |
| B | ASP181 |
| B | HIS183 |
| B | SER202 |
| B | LEU203 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue K B 403 |
| Chain | Residue |
| B | TYR192 |
| B | ARG195 |
| B | VAL198 |
| B | PHE227 |
| B | HOH538 |
| B | HOH553 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue 9RB B 404 |
| Chain | Residue |
| A | LEU340 |
| A | PHE343 |
| B | THR24 |
| B | ASP101 |
| B | HIS143 |
| B | HIS144 |
| B | PHE153 |
| B | ASP181 |
| B | HIS183 |
| B | PHE209 |
| B | ASP269 |
| B | TYR313 |
| B | ZN401 |
| B | HOH502 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q48935","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27756124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27951649","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LI3","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5G0X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Polarizes the scissile carbonyl of the substrate","evidences":[{"source":"UniProtKB","id":"Q48935","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
