2DEY
Crystal structure of human peptidylarginine deiminase 4 in complex with histone H4 N-terminal tail including Arg3
Functional Information from GO Data
Chain | GOid | namespace | contents |
X | 0004668 | molecular_function | protein-arginine deiminase activity |
X | 0005509 | molecular_function | calcium ion binding |
X | 0005515 | molecular_function | protein binding |
X | 0005634 | cellular_component | nucleus |
X | 0005654 | cellular_component | nucleoplasm |
X | 0005737 | cellular_component | cytoplasm |
X | 0005829 | cellular_component | cytosol |
X | 0006325 | biological_process | chromatin organization |
X | 0006334 | biological_process | nucleosome assembly |
X | 0006338 | biological_process | chromatin remodeling |
X | 0016787 | molecular_function | hydrolase activity |
X | 0019827 | biological_process | stem cell population maintenance |
X | 0032991 | cellular_component | protein-containing complex |
X | 0036211 | biological_process | protein modification process |
X | 0042802 | molecular_function | identical protein binding |
X | 0043687 | biological_process | post-translational protein modification |
X | 0045087 | biological_process | innate immune response |
X | 0046872 | molecular_function | metal ion binding |
X | 0140794 | molecular_function | histone arginine deiminase activity |
X | 0140795 | molecular_function | histone H3R2 arginine deiminase activity |
X | 0140796 | molecular_function | histone H3R8 arginine deiminase activity |
X | 0140797 | molecular_function | histone H3R17 arginine deiminase activity |
X | 0140798 | molecular_function | histone H3R26 arginine deiminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA X 900 |
Chain | Residue |
X | GLN349 |
X | GLU353 |
X | PHE407 |
X | LEU410 |
X | GLU411 |
X | HOH928 |
X | HOH1034 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA X 901 |
Chain | Residue |
X | ASP157 |
X | ASP165 |
X | ASP176 |
X | ASP179 |
X | ASN153 |
X | ASP155 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA X 902 |
Chain | Residue |
X | ASP155 |
X | ASP157 |
X | ASP179 |
X | ASP388 |
X | HOH1024 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA X 903 |
Chain | Residue |
X | GLU351 |
X | ASP369 |
X | SER370 |
X | ASN373 |
X | HOH1040 |
X | HOH1058 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA X 904 |
Chain | Residue |
X | ASP165 |
X | ASP168 |
X | GLU170 |
X | HOH1017 |
X | HOH1028 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 X 905 |
Chain | Residue |
A | LYS5 |
X | SER402 |
X | GLY403 |
X | ARG441 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 X 906 |
Chain | Residue |
X | ARG495 |
X | SER496 |
X | LYS499 |
X | LYS615 |
X | HOH932 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 X 907 |
Chain | Residue |
X | LYS525 |
X | LYS527 |
X | ASN528 |
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 |
X | ASP350 | |
X | HIS471 | |
X | ASP473 | |
X | 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 |
X | ASN153 | |
X | GLU351 | |
X | GLU353 | |
X | ASP369 | |
X | SER370 | |
X | ASN373 | |
X | ASP388 | |
X | PHE407 | |
X | LEU410 | |
X | GLU411 | |
X | ASP155 | |
X | ASP157 | |
X | ASP165 | |
X | ASP168 | |
X | GLU170 | |
X | ASP176 | |
X | ASP179 | |
X | GLN349 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21882827 |
Chain | Residue | Details |
X | ARG374 | |
X | ARG639 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: Citrulline => ECO:0000269|PubMed:20201080 |
Chain | Residue | Details |
X | ARG205 | |
X | ARG212 | |
X | ARG218 | |
X | ARG372 | |
X | ARG374 | |
X | ARG383 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1wd8 |
Chain | Residue | Details |
X | ASP473 | |
X | ASP350 | |
X | ALA645 | |
X | HIS471 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 594 |
Chain | Residue | Details |
X | ASP350 | electrostatic stabiliser |
X | HIS471 | proton acceptor, proton donor |
X | ASP473 | electrostatic stabiliser |
X | ALA645 | nucleofuge, nucleophile, proton acceptor, proton donor |