Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0002250biological_processadaptive immune response
A0002376biological_processimmune system process
A0004053molecular_functionarginase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006525biological_processarginine metabolic process
A0006527biological_processL-arginine catabolic process
A0009624biological_processresponse to nematode
A0016787molecular_functionhydrolase activity
A0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A0030145molecular_functionmanganese ion binding
A0035578cellular_componentazurophil granule lumen
A0035580cellular_componentspecific granule lumen
A0042127biological_processregulation of cell population proliferation
A0042130biological_processnegative regulation of T cell proliferation
A0042832biological_processdefense response to protozoan
A0045087biological_processinnate immune response
A0046007biological_processnegative regulation of activated T cell proliferation
A0046872molecular_functionmetal ion binding
A0060336biological_processnegative regulation of type II interferon-mediated signaling pathway
A0070965biological_processpositive regulation of neutrophil mediated killing of fungus
A2000552biological_processnegative regulation of T-helper 2 cell cytokine production
B0000050biological_processurea cycle
B0002250biological_processadaptive immune response
B0002376biological_processimmune system process
B0004053molecular_functionarginase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006525biological_processarginine metabolic process
B0006527biological_processL-arginine catabolic process
B0009624biological_processresponse to nematode
B0016787molecular_functionhydrolase activity
B0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B0030145molecular_functionmanganese ion binding
B0035578cellular_componentazurophil granule lumen
B0035580cellular_componentspecific granule lumen
B0042127biological_processregulation of cell population proliferation
B0042130biological_processnegative regulation of T cell proliferation
B0042832biological_processdefense response to protozoan
B0045087biological_processinnate immune response
B0046007biological_processnegative regulation of activated T cell proliferation
B0046872molecular_functionmetal ion binding
B0060336biological_processnegative regulation of type II interferon-mediated signaling pathway
B0070965biological_processpositive regulation of neutrophil mediated killing of fungus
B2000552biological_processnegative regulation of T-helper 2 cell cytokine production
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 514
ChainResidue
AASP124
AHIS126
AASP232
AASP234
AMN515
A5AB551

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 515
ChainResidue
AASP232
AMN514
A5AB551
AHIS101
AASP124
AASP128

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 5AB A 551
ChainResidue
AHIS101
AASP124
AHIS126
AASP128
AASN130
ASER137
AHIS141
AASP183
AGLU186
AASP232
AASP234
AGLU277
AHOH337
AHOH352
AHOH413
AHOH444
AMN514
AMN515
AHOH582
AHOH585

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 514
ChainResidue
BASP124
BHIS126
BASP232
BASP234
BMN515
B5AB552

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 515
ChainResidue
BHIS101
BASP124
BASP128
BASP232
BMN514
B5AB552

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 5AB B 552
ChainResidue
BHIS101
BASP124
BHIS126
BASP128
BASN130
BSER137
BHIS141
BASP183
BGLU186
BASP232
BASP234
BGLU277
BHOH323
BHOH368
BHOH429
BHOH454
BHOH489
BMN514
BMN515
BHOH530

Functional Information from PROSITE/UniProt
site_idPS01053
Number of Residues22
DetailsARGINASE_1 Arginase family signature. SFDVDgldPsftPAtgtpvvgG
ChainResidueDetails
ASER230-GLY251

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P53608","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P78540","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q61176","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q61176","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon