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 | 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: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | HIS179 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00538 |
Chain | Residue | Details |
A | ASP181 | |
A | HIS240 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | SER309 |