7XE3
Crystal structure of LSD2 in complex with cis-4-Br-2,5-F2-PCPA (S1024)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000786 | cellular_component | nucleosome |
A | 0003682 | molecular_function | chromatin binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005694 | cellular_component | chromosome |
A | 0006325 | biological_process | chromatin organization |
A | 0006338 | biological_process | chromatin remodeling |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0032452 | molecular_function | histone demethylase activity |
A | 0032453 | molecular_function | histone H3K4 demethylase activity |
A | 0042393 | molecular_function | histone binding |
A | 0044726 | biological_process | epigenetic programing of female pronucleus |
A | 0046872 | molecular_function | metal ion binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0071514 | biological_process | genomic imprinting |
A | 0071949 | molecular_function | FAD binding |
A | 0140682 | molecular_function | FAD-dependent H3K4me/H3K4me3 demethylase activity |
B | 0000786 | cellular_component | nucleosome |
B | 0003682 | molecular_function | chromatin binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005694 | cellular_component | chromosome |
B | 0006325 | biological_process | chromatin organization |
B | 0006338 | biological_process | chromatin remodeling |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0032452 | molecular_function | histone demethylase activity |
B | 0032453 | molecular_function | histone H3K4 demethylase activity |
B | 0042393 | molecular_function | histone binding |
B | 0044726 | biological_process | epigenetic programing of female pronucleus |
B | 0046872 | molecular_function | metal ion binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0071514 | biological_process | genomic imprinting |
B | 0071949 | molecular_function | FAD binding |
B | 0140682 | molecular_function | FAD-dependent H3K4me/H3K4me3 demethylase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 120 |
Details | ZN_FING: CW-type => ECO:0000255|PROSITE-ProRule:PRU00454 |
Chain | Residue | Details |
A | ASP133-VAL193 | |
B | ASP133-VAL193 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, ECO:0007744|PDB:6R25 |
Chain | Residue | Details |
A | CYS53 | |
A | GLN803 | |
B | CYS53 | |
B | CYS58 | |
B | CYS65 | |
B | CYS73 | |
B | HIS84 | |
B | HIS90 | |
B | CYS92 | |
B | CYS95 | |
B | VAL598 | |
A | CYS58 | |
B | GLN803 | |
A | CYS65 | |
A | CYS73 | |
A | HIS84 | |
A | HIS90 | |
A | CYS92 | |
A | CYS95 | |
A | VAL598 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00454, ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, ECO:0007744|PDB:6R25 |
Chain | Residue | Details |
A | CYS142 | |
A | CYS147 | |
A | CYS169 | |
A | CYS185 | |
B | CYS142 | |
B | CYS147 | |
B | CYS169 | |
B | CYS185 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255, ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:23357850, ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, ECO:0007744|PDB:4GU0, ECO:0007744|PDB:4GU1, ECO:0007744|PDB:4GUR, ECO:0007744|PDB:4GUS, ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, ECO:0007744|PDB:4HSU, ECO:0007744|PDB:6R1U, ECO:0007744|PDB:6R25 |
Chain | Residue | Details |
A | LYS383 | |
B | LYS383 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23260659, ECO:0000269|PubMed:23266887, ECO:0000269|PubMed:30970244, ECO:0007744|PDB:4FWE, ECO:0007744|PDB:4FWF, ECO:0007744|PDB:4FWJ, ECO:0007744|PDB:4GU1, ECO:0007744|PDB:4GUS, ECO:0007744|PDB:4GUT, ECO:0007744|PDB:4GUU, ECO:0007744|PDB:6R1U, ECO:0007744|PDB:6R25 |
Chain | Residue | Details |
A | GLU795 | |
B | GLU795 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER247 | |
B | SER247 |