3MFW
Crystal structure of human arginase I in complex with L-2-aminohistidine and sulphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000050 | biological_process | urea cycle |
A | 0002250 | biological_process | adaptive immune response |
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 | 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 | 0019547 | biological_process | arginine catabolic process to ornithine |
A | 0030145 | molecular_function | manganese ion binding |
A | 0035578 | cellular_component | azurophil granule lumen |
A | 0035580 | cellular_component | specific granule lumen |
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 | 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 | 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 | 0019547 | biological_process | arginine catabolic process to ornithine |
B | 0030145 | molecular_function | manganese ion binding |
B | 0035578 | cellular_component | azurophil granule lumen |
B | 0035580 | cellular_component | specific granule lumen |
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 | 12 |
Details | BINDING SITE FOR RESIDUE SO4 A 551 |
Chain | Residue |
A | HIS101 |
A | B3U600 |
A | MN5362 |
A | MN5363 |
A | ASP124 |
A | HIS126 |
A | ASP128 |
A | HIS141 |
A | ASP232 |
A | ASP234 |
A | THR246 |
A | GLU277 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE B3U A 600 |
Chain | Residue |
A | HIS126 |
A | ASP128 |
A | ASN130 |
A | SER137 |
A | HIS141 |
A | GLY142 |
A | ASP183 |
A | GLU186 |
A | THR246 |
A | HOH354 |
A | HOH361 |
A | HOH406 |
A | HOH414 |
A | HOH508 |
A | SO4551 |
A | HOH581 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 5362 |
Chain | Residue |
A | ASP124 |
A | HIS126 |
A | ASP232 |
A | ASP234 |
A | SO4551 |
A | MN5363 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 5363 |
Chain | Residue |
A | HIS101 |
A | ASP124 |
A | ASP128 |
A | ASP232 |
A | SO4551 |
A | MN5362 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 B 552 |
Chain | Residue |
B | HIS101 |
B | ASP124 |
B | HIS126 |
B | ASP128 |
B | HIS141 |
B | ASP232 |
B | ASP234 |
B | GLU277 |
B | B3U601 |
B | MN6362 |
B | MN6363 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE B3U B 601 |
Chain | Residue |
B | HIS126 |
B | ASP128 |
B | ASN130 |
B | SER137 |
B | HIS141 |
B | GLY142 |
B | ASP183 |
B | GLU186 |
B | THR246 |
B | HOH352 |
B | HOH381 |
B | HOH383 |
B | HOH415 |
B | HOH508 |
B | HOH514 |
B | SO4552 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 6362 |
Chain | Residue |
B | ASP124 |
B | HIS126 |
B | ASP232 |
B | ASP234 |
B | SO4552 |
B | MN6363 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 6363 |
Chain | Residue |
B | HIS101 |
B | ASP124 |
B | ASP128 |
B | ASP232 |
B | SO4552 |
B | MN6362 |
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
Chain | Residue | Details |
A | HIS101 | |
B | ASP128 | |
B | ASP232 | |
B | ASP234 | |
A | ASP124 | |
A | HIS126 | |
A | ASP128 | |
A | ASP232 | |
A | ASP234 | |
B | HIS101 | |
B | ASP124 | |
B | HIS126 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0, ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3THJ |
Chain | Residue | Details |
A | SER137 | |
A | ASP183 | |
B | SER137 | |
B | ASP183 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P53608 |
Chain | Residue | Details |
A | THR246 | |
B | THR246 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P78540 |
Chain | Residue | Details |
A | GLU277 | |
B | GLU277 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q61176 |
Chain | Residue | Details |
A | LYS17 | |
A | LYS75 | |
B | LYS17 | |
B | LYS75 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER62 | |
A | SER163 | |
A | SER217 | |
B | SER62 | |
B | SER163 | |
B | SER217 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q61176 |
Chain | Residue | Details |
A | SER72 | |
B | SER72 |