4N25
Crystal structure of Protein Arginine Deiminase 2 (250 uM Ca2+)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000791 | cellular_component | euchromatin |
A | 0004668 | molecular_function | protein-arginine deiminase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006338 | biological_process | chromatin remodeling |
A | 0016787 | molecular_function | hydrolase activity |
A | 0021762 | biological_process | substantia nigra development |
A | 0030331 | molecular_function | nuclear estrogen receptor binding |
A | 0030520 | biological_process | estrogen receptor signaling pathway |
A | 0035578 | cellular_component | azurophil granule lumen |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0045815 | biological_process | transcription initiation-coupled chromatin remodeling |
A | 0046872 | molecular_function | metal ion binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070100 | biological_process | negative regulation of chemokine-mediated signaling pathway |
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 |
A | 0140809 | molecular_function | histone H4R3 arginine deiminase activity |
A | 0140810 | molecular_function | histone H1R54 arginine deiminase activity |
A | 0140811 | molecular_function | histone H2AR3 arginine deiminase activity |
A | 1901624 | biological_process | negative regulation of lymphocyte chemotaxis |
A | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MRD A 701 |
Chain | Residue |
A | SER434 |
A | GLU461 |
A | LEU462 |
A | TRP550 |
A | HOH953 |
A | HOH1116 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MPD A 702 |
Chain | Residue |
A | HOH1151 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 703 |
Chain | Residue |
A | GLU511 |
A | ALA512 |
A | HOH927 |
A | GLY508 |
A | HIS509 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 704 |
Chain | Residue |
A | ASP123 |
A | ASP125 |
A | ASP127 |
A | VAL129 |
A | GLU131 |
A | HOH1161 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 705 |
Chain | Residue |
A | ASN154 |
A | ASP156 |
A | ASP166 |
A | ASP177 |
A | ASP180 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 706 |
Chain | Residue |
A | ASP156 |
A | ASP180 |
A | ASP389 |
A | HOH945 |
A | HOH1155 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 707 |
Chain | Residue |
A | ASP166 |
A | ASP169 |
A | LYS171 |
A | HOH1073 |
A | HOH1127 |
A | HOH1175 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 708 |
Chain | Residue |
A | GLU354 |
A | PHE408 |
A | LEU411 |
A | GLU412 |
A | HOH892 |
A | HOH1170 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD A 709 |
Chain | Residue |
A | PHE320 |
A | GLN350 |
A | ASN590 |
A | MET591 |
A | ILE592 |
A | PRO601 |
A | ASP634 |
A | THR649 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:25621824 |
Chain | Residue | Details |
A | CYS647 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25621824, ECO:0007744|PDB:4N20, ECO:0007744|PDB:4N22, ECO:0007744|PDB:4N24, ECO:0007744|PDB:4N25, ECO:0007744|PDB:4N26, ECO:0007744|PDB:4N28, ECO:0007744|PDB:4N2A, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2C, ECO:0007744|PDB:4N2F, ECO:0007744|PDB:4N2G, ECO:0007744|PDB:4N2H, ECO:0007744|PDB:4N2I, ECO:0007744|PDB:4N2L, ECO:0007744|PDB:4N2M, ECO:0007744|PDB:4N2N |
Chain | Residue | Details |
A | ASP123 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25621824, ECO:0007744|PDB:4N20, ECO:0007744|PDB:4N22, ECO:0007744|PDB:4N24, ECO:0007744|PDB:4N26, ECO:0007744|PDB:4N28, ECO:0007744|PDB:4N2A, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2C, ECO:0007744|PDB:4N2D, ECO:0007744|PDB:4N2E, ECO:0007744|PDB:4N2F, ECO:0007744|PDB:4N2G, ECO:0007744|PDB:4N2H, ECO:0007744|PDB:4N2I, ECO:0007744|PDB:4N2K, ECO:0007744|PDB:4N2L, ECO:0007744|PDB:4N2M, ECO:0007744|PDB:4N2N |
Chain | Residue | Details |
A | ASP125 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25621824, ECO:0007744|PDB:4N20, ECO:0007744|PDB:4N22, ECO:0007744|PDB:4N24, ECO:0007744|PDB:4N25, ECO:0007744|PDB:4N26, ECO:0007744|PDB:4N28, ECO:0007744|PDB:4N2A, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2C, ECO:0007744|PDB:4N2D, ECO:0007744|PDB:4N2E, ECO:0007744|PDB:4N2F, ECO:0007744|PDB:4N2G, ECO:0007744|PDB:4N2H, ECO:0007744|PDB:4N2I, ECO:0007744|PDB:4N2K, ECO:0007744|PDB:4N2L, ECO:0007744|PDB:4N2M, ECO:0007744|PDB:4N2N |
Chain | Residue | Details |
A | ASP127 | |
A | VAL129 | |
A | GLU131 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25621824, ECO:0007744|PDB:4N25, ECO:0007744|PDB:4N26, ECO:0007744|PDB:4N28, ECO:0007744|PDB:4N2A, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2E, ECO:0007744|PDB:4N2G, ECO:0007744|PDB:4N2I, ECO:0007744|PDB:4N2L, ECO:0007744|PDB:4N2N |
Chain | Residue | Details |
A | ASN154 | |
A | ASP389 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25621824, ECO:0007744|PDB:4N25, ECO:0007744|PDB:4N26, ECO:0007744|PDB:4N28, ECO:0007744|PDB:4N2A, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2C, ECO:0007744|PDB:4N2E, ECO:0007744|PDB:4N2G, ECO:0007744|PDB:4N2I, ECO:0007744|PDB:4N2L, ECO:0007744|PDB:4N2N |
Chain | Residue | Details |
A | ASP156 | |
A | ASP180 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25621824, ECO:0007744|PDB:4N26, ECO:0007744|PDB:4N28, ECO:0007744|PDB:4N2A, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2C, ECO:0007744|PDB:4N2E, ECO:0007744|PDB:4N2G, ECO:0007744|PDB:4N2I, ECO:0007744|PDB:4N2L, ECO:0007744|PDB:4N2N |
Chain | Residue | Details |
A | GLU158 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25621824, ECO:0007744|PDB:4N25, ECO:0007744|PDB:4N26, ECO:0007744|PDB:4N2A, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2C, ECO:0007744|PDB:4N2E, ECO:0007744|PDB:4N2I, ECO:0007744|PDB:4N2L |
Chain | Residue | Details |
A | ASP166 | |
A | ASP169 | |
A | LYS171 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:4N25, ECO:0007744|PDB:4N26, ECO:0007744|PDB:4N28, ECO:0007744|PDB:4N2A, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2E, ECO:0007744|PDB:4N2G, ECO:0007744|PDB:4N2L, ECO:0007744|PDB:4N2N |
Chain | Residue | Details |
A | ASP177 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25621824, ECO:0007744|PDB:4N28, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2C, ECO:0007744|PDB:4N2I |
Chain | Residue | Details |
A | GLU354 |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25621824, ECO:0007744|PDB:4N28, ECO:0007744|PDB:4N2B, ECO:0007744|PDB:4N2C, ECO:0007744|PDB:4N2E, ECO:0007744|PDB:4N2I |
Chain | Residue | Details |
A | PHE408 | |
A | LEU411 | |
A | GLU412 |