Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4IE1

Crystal structure of human Arginase-1 complexed with inhibitor 1h

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0002250biological_processadaptive immune response
A0004053molecular_functionarginase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006525biological_processarginine metabolic process
A0006527biological_processarginine catabolic process
A0016787molecular_functionhydrolase activity
A0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A0019547biological_processarginine catabolic process to ornithine
A0030145molecular_functionmanganese ion binding
A0035578cellular_componentazurophil granule lumen
A0035580cellular_componentspecific granule lumen
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
B0004053molecular_functionarginase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006525biological_processarginine metabolic process
B0006527biological_processarginine catabolic process
B0016787molecular_functionhydrolase activity
B0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B0019547biological_processarginine catabolic process to ornithine
B0030145molecular_functionmanganese ion binding
B0035578cellular_componentazurophil granule lumen
B0035580cellular_componentspecific granule lumen
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 Residues19
DetailsBINDING SITE FOR RESIDUE 1EC A 401
ChainResidue
AHIS101
AASP232
AASP234
ATHR246
AGLU277
AMN402
AMN403
AHOH520
AHOH530
AHOH558
AHOH607
AASP124
AHIS126
AASP128
AASN130
ATHR136
ASER137
AHIS141
AASP183

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AASP124
AHIS126
AASP232
AASP234
A1EC401
AMN403

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 403
ChainResidue
AHIS101
AASP124
AASP128
AASP232
A1EC401
AMN402

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 1EC B 501
ChainResidue
AARG222
BHIS101
BASP124
BHIS126
BASP128
BASN130
BTHR136
BSER137
BHIS141
BASP183
BASP232
BASP234
BTHR246
BGLU277
BMN502
BMN503
BHOH656
BHOH657
BHOH659
BHOH662
BHOH668

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 502
ChainResidue
BASP124
BHIS126
BASP232
BASP234
B1EC501
BMN503

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 503
ChainResidue
BHIS101
BASP124
BASP128
BASP232
B1EC501
BMN502

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: BINDING => ECO:0000269|PubMed:16141327, ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323, ECO:0000269|PubMed:18802628, ECO:0000269|PubMed:21728378, ECO:0007744|PDB:1WVA, ECO:0007744|PDB:1WVB, ECO:0007744|PDB:2AEB, ECO:0007744|PDB:2PHA, ECO:0007744|PDB:2PHO, ECO:0007744|PDB:2PLL, ECO:0007744|PDB:2ZAV, ECO:0007744|PDB:3DJ8, ECO:0007744|PDB:3E6K, ECO:0007744|PDB:3E6V, ECO:0007744|PDB:3F80, ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0, ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP4, ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3MFV, ECO:0007744|PDB:3MFW, ECO:0007744|PDB:3MJL, ECO:0007744|PDB:3SJT, ECO:0007744|PDB:3SKK, ECO:0007744|PDB:4FCI, ECO:0007744|PDB:4GSZ, ECO:0007744|PDB:4GWC, ECO:0007744|PDB:4GWD, ECO:0007744|PDB:4HWW, ECO:0007744|PDB:4HXQ, ECO:0007744|PDB:4IE1
ChainResidueDetails
AHIS101
BASP128
BASP232
BASP234
AASP124
AHIS126
AASP128
AASP232
AASP234
BHIS101
BASP124
BHIS126

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0, ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3THJ
ChainResidueDetails
ASER137
AASP183
BSER137
BASP183

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P53608
ChainResidueDetails
ATHR246
BTHR246

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P78540
ChainResidueDetails
AGLU277
BGLU277

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q61176
ChainResidueDetails
ALYS17
ALYS75
BLYS17
BLYS75

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER62
ASER163
ASER217
BSER62
BSER163
BSER217

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q61176
ChainResidueDetails
ASER72
BSER72

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon