4N2B
Crystal structure of Protein Arginine Deiminase 2 (10 mM 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 | intracellular 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 | 0140798 | molecular_function | histone H3R26 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 | 9 |
| Details | BINDING SITE FOR RESIDUE MPD A 701 |
| Chain | Residue |
| A | SER433 |
| A | SER434 |
| A | PRO436 |
| A | GLU461 |
| A | LEU462 |
| A | TRP550 |
| A | HOH983 |
| A | HOH1311 |
| A | HOH1493 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 702 |
| Chain | Residue |
| A | GLU199 |
| A | LEU282 |
| A | HOH1290 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD A 703 |
| Chain | Residue |
| A | TYR216 |
| A | GLU218 |
| A | HIS237 |
| A | VAL239 |
| A | LYS240 |
| A | PHE250 |
| A | HOH1468 |
| 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 | HOH954 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 705 |
| Chain | Residue |
| A | ASN154 |
| A | ASP156 |
| A | GLU158 |
| A | ASP166 |
| A | ASP177 |
| A | ASP180 |
| A | CA709 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 706 |
| Chain | Residue |
| A | ASP166 |
| A | ASP169 |
| A | LYS171 |
| A | HOH826 |
| A | HOH844 |
| A | HOH886 |
| A | HOH900 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 707 |
| Chain | Residue |
| A | GLN350 |
| A | GLU354 |
| A | PHE408 |
| A | LEU411 |
| A | GLU412 |
| A | HOH819 |
| A | HOH952 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD A 708 |
| Chain | Residue |
| A | MET575 |
| A | HOH956 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CA A 709 |
| Chain | Residue |
| A | ASP156 |
| A | GLU158 |
| A | ASP180 |
| A | LYS363 |
| A | ASP389 |
| A | CA705 |
| A | HOH850 |
| A | HOH857 |
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 | GLU131 | |
| A | ASP127 | |
| A | VAL129 |
| 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 | ASP389 | |
| A | ASN154 |
| 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 | ASP180 | |
| A | ASP156 |
| 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 | ASP169 | |
| A | LYS171 | |
| A | ASP166 |
| 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 | LEU411 | |
| A | GLU412 | |
| A | PHE408 |
