3APN
Crystal structure of the human wild-type PAD4 protein
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 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 | CYS645 |
| 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 | CYS645 | nucleofuge, nucleophile, proton acceptor, proton donor |
