2PLL
Crystal structure of perdeuterated human arginase I
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000050 | biological_process | urea cycle |
| A | 0002250 | biological_process | adaptive immune response |
| A | 0002376 | biological_process | immune system process |
| A | 0004053 | molecular_function | arginase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0009624 | biological_process | response to nematode |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0035578 | cellular_component | azurophil granule lumen |
| A | 0035580 | cellular_component | specific granule lumen |
| A | 0042127 | biological_process | regulation of cell population proliferation |
| A | 0042130 | biological_process | negative regulation of T cell proliferation |
| A | 0042832 | biological_process | defense response to protozoan |
| A | 0045087 | biological_process | innate immune response |
| A | 0046007 | biological_process | negative regulation of activated T cell proliferation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0060336 | biological_process | negative regulation of type II interferon-mediated signaling pathway |
| A | 0070965 | biological_process | positive regulation of neutrophil mediated killing of fungus |
| A | 2000552 | biological_process | negative regulation of T-helper 2 cell cytokine production |
| B | 0000050 | biological_process | urea cycle |
| B | 0002250 | biological_process | adaptive immune response |
| B | 0002376 | biological_process | immune system process |
| B | 0004053 | molecular_function | arginase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0009624 | biological_process | response to nematode |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0035578 | cellular_component | azurophil granule lumen |
| B | 0035580 | cellular_component | specific granule lumen |
| B | 0042127 | biological_process | regulation of cell population proliferation |
| B | 0042130 | biological_process | negative regulation of T cell proliferation |
| B | 0042832 | biological_process | defense response to protozoan |
| B | 0045087 | biological_process | innate immune response |
| B | 0046007 | biological_process | negative regulation of activated T cell proliferation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0060336 | biological_process | negative regulation of type II interferon-mediated signaling pathway |
| B | 0070965 | biological_process | positive regulation of neutrophil mediated killing of fungus |
| B | 2000552 | biological_process | negative regulation of T-helper 2 cell cytokine production |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 461 |
| Chain | Residue |
| B | ASP124 |
| B | HIS126 |
| B | ASP232 |
| B | ASP234 |
| B | MN462 |
| B | ABH556 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 462 |
| Chain | Residue |
| B | ASP232 |
| B | MN461 |
| B | ABH556 |
| B | HIS101 |
| B | ASP124 |
| B | ASP128 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 463 |
| Chain | Residue |
| A | ASP124 |
| A | HIS126 |
| A | ASP232 |
| A | ASP234 |
| A | MN464 |
| A | ABH555 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 464 |
| Chain | Residue |
| A | HIS101 |
| A | ASP124 |
| A | ASP128 |
| A | ASP232 |
| A | MN463 |
| A | ABH555 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ABH A 555 |
| Chain | Residue |
| A | HIS101 |
| A | ASP124 |
| A | HIS126 |
| A | ASP128 |
| A | ASN130 |
| A | SER137 |
| A | HIS141 |
| A | ASP183 |
| A | GLU186 |
| A | ASP232 |
| A | ASP234 |
| A | GLU277 |
| A | MN463 |
| A | MN464 |
| A | HOH569 |
| A | HOH581 |
| A | HOH624 |
| A | HOH639 |
| A | HOH648 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ABH B 556 |
| Chain | Residue |
| B | HIS101 |
| B | ASP124 |
| B | HIS126 |
| B | ASP128 |
| B | ASN130 |
| B | SER137 |
| B | HIS141 |
| B | ASP183 |
| B | GLU186 |
| B | ASP232 |
| B | ASP234 |
| B | GLU277 |
| B | MN461 |
| B | MN462 |
| B | HOH558 |
| B | HOH653 |
| B | HOH681 |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. SFDVDgldPsftPAtgtpvvgG |
| Chain | Residue | Details |
| A | SER230-GLY251 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16141327","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17469833","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17562323","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18802628","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21728378","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WVA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WVB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AEB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PHA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PHO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZAV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DJ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3E6K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3E6V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3F80","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GMZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GN0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LP4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LP7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MFW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MJL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SJT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SKK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FCI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GSZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GWC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GWD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HWW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HXQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IE1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3GMZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GN0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LP7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3THJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P53608","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P78540","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q61176","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q61176","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| A | GLU277 | |
| A | ASP128 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| B | GLU277 | |
| B | ASP128 |
