4X8G
Crystal structure of human peptidylarginine deiminase type4 (PAD4) in complex with GSK199
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004668 | molecular_function | protein-arginine deiminase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006325 | biological_process | chromatin organization |
A | 0006334 | biological_process | nucleosome assembly |
A | 0006338 | biological_process | chromatin remodeling |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019827 | biological_process | stem cell population maintenance |
A | 0032991 | cellular_component | protein-containing complex |
A | 0036211 | biological_process | protein modification process |
A | 0042802 | molecular_function | identical protein binding |
A | 0043687 | biological_process | post-translational protein modification |
A | 0045087 | biological_process | innate immune response |
A | 0046872 | molecular_function | metal ion binding |
A | 0140794 | molecular_function | histone arginine deiminase activity |
A | 0140795 | molecular_function | histone H3R2 arginine deiminase activity |
A | 0140796 | molecular_function | histone H3R8 arginine deiminase activity |
A | 0140797 | molecular_function | histone H3R17 arginine deiminase activity |
A | 0140798 | molecular_function | histone H3R26 arginine deiminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 701 |
Chain | Residue |
A | GLU353 |
A | PHE407 |
A | LEU410 |
A | GLU411 |
A | HOH818 |
A | HOH819 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 702 |
Chain | Residue |
A | ASP165 |
A | ASP176 |
A | ASP179 |
A | ASN153 |
A | ASP155 |
A | ASP157 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CA A 703 |
Chain | Residue |
A | ASP155 |
A | ASP157 |
A | ASP179 |
A | LYS362 |
A | ASP388 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA A 704 |
Chain | Residue |
A | ASP165 |
A | ASP168 |
A | GLU170 |
A | HOH813 |
A | HOH821 |
A | HOH822 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue 3Z0 A 705 |
Chain | Residue |
A | VAL469 |
A | HIS471 |
A | ASP473 |
A | GLU474 |
A | ALA581 |
A | PHE582 |
A | PHE583 |
A | PRO584 |
A | ASN585 |
A | ASN588 |
A | VAL643 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:15247907 |
Chain | Residue | Details |
A | ASP350 | |
A | HIS471 | |
A | ASP473 | |
A | ALA645 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15247907, ECO:0000269|PubMed:16567635, ECO:0000269|PubMed:17002273 |
Chain | Residue | Details |
A | ASN153 | |
A | GLU351 | |
A | GLU353 | |
A | ASP369 | |
A | SER370 | |
A | ASN373 | |
A | ASP388 | |
A | PHE407 | |
A | LEU410 | |
A | GLU411 | |
A | ASP155 | |
A | ASP157 | |
A | ASP165 | |
A | ASP168 | |
A | GLU170 | |
A | ASP176 | |
A | ASP179 | |
A | GLN349 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21882827 |
Chain | Residue | Details |
A | ARG374 | |
A | ARG639 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: Citrulline => ECO:0000269|PubMed:20201080 |
Chain | Residue | Details |
A | ARG205 | |
A | ARG212 | |
A | ARG218 | |
A | ARG372 | |
A | ARG374 | |
A | ARG383 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 594 |
Chain | Residue | Details |
A | ASP350 | electrostatic stabiliser |
A | HIS471 | proton acceptor, proton donor |
A | ASP473 | electrostatic stabiliser |
A | ALA645 | nucleofuge, nucleophile, proton acceptor, proton donor |