3SJT
Crystal structure of human arginase I in complex with the inhibitor Me-ABH, Resolution 1.60 A, twinned structure
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 A 514 |
Chain | Residue |
A | ASP124 |
A | HIS126 |
A | ASP232 |
A | ASP234 |
A | MN515 |
A | 5AB551 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 515 |
Chain | Residue |
A | ASP232 |
A | MN514 |
A | 5AB551 |
A | HIS101 |
A | ASP124 |
A | ASP128 |
site_id | AC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE 5AB A 551 |
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 | HOH337 |
A | HOH352 |
A | HOH413 |
A | HOH444 |
A | MN514 |
A | MN515 |
A | HOH582 |
A | HOH585 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 514 |
Chain | Residue |
B | ASP124 |
B | HIS126 |
B | ASP232 |
B | ASP234 |
B | MN515 |
B | 5AB552 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 515 |
Chain | Residue |
B | HIS101 |
B | ASP124 |
B | ASP128 |
B | ASP232 |
B | MN514 |
B | 5AB552 |
site_id | AC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE 5AB B 552 |
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 | HOH323 |
B | HOH368 |
B | HOH429 |
B | HOH454 |
B | HOH489 |
B | MN514 |
B | MN515 |
B | HOH530 |
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 |