4BU2
60S ribosomal protein L27A histidine hydroxylase (MINA53) in complex with Ni(II) and 2-oxoglutarate (2OG)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003714 | molecular_function | transcription corepressor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005667 | cellular_component | transcription regulator complex |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018126 | biological_process | protein hydroxylation |
| A | 0032452 | molecular_function | histone demethylase activity |
| A | 0032453 | molecular_function | histone H3K4 demethylase activity |
| A | 0036139 | molecular_function | peptidyl-histidine dioxygenase activity |
| A | 0042254 | biological_process | ribosome biogenesis |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0051864 | molecular_function | histone H3K36 demethylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI A 601 |
| Chain | Residue |
| A | HIS179 |
| A | ASP181 |
| A | HIS240 |
| A | AKG701 |
| A | HOH2053 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI A 602 |
| Chain | Residue |
| A | HIS195 |
| A | GLU223 |
| A | ASP243 |
| A | HOH2122 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AKG A 701 |
| Chain | Residue |
| A | TYR167 |
| A | GLY175 |
| A | LEU176 |
| A | HIS179 |
| A | ASP181 |
| A | LYS194 |
| A | HIS240 |
| A | HIS253 |
| A | THR255 |
| A | NI601 |
| A | HOH2053 |
| A | HOH2054 |
| A | HOH2056 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 901 |
| Chain | Residue |
| A | GLU152 |
| A | LYS153 |
| A | HOH2045 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 902 |
| Chain | Residue |
| A | ASN165 |
| A | TYR167 |
| A | ASP181 |
| A | THR255 |
| A | HOH2050 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 903 |
| Chain | Residue |
| A | LYS144 |
| A | ASP145 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 904 |
| Chain | Residue |
| A | SER160 |
| A | LEU161 |
| A | MSE330 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00538","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
