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6V7E

Human Arginase1 Complexed with Bicyclic Inhibitor Compound 12

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
C0000050biological_processurea cycle
C0002250biological_processadaptive immune response
C0004053molecular_functionarginase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006525biological_processarginine metabolic process
C0006527biological_processarginine catabolic process
C0016787molecular_functionhydrolase activity
C0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
C0019547biological_processarginine catabolic process to ornithine
C0030145molecular_functionmanganese ion binding
C0035578cellular_componentazurophil granule lumen
C0035580cellular_componentspecific granule lumen
C0042130biological_processnegative regulation of T cell proliferation
C0042832biological_processdefense response to protozoan
C0045087biological_processinnate immune response
C0046007biological_processnegative regulation of activated T cell proliferation
C0046872molecular_functionmetal ion binding
C0060336biological_processnegative regulation of type II interferon-mediated signaling pathway
C0070965biological_processpositive regulation of neutrophil mediated killing of fungus
C2000552biological_processnegative regulation of T-helper 2 cell cytokine production
D0000050biological_processurea cycle
D0002250biological_processadaptive immune response
D0004053molecular_functionarginase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006525biological_processarginine metabolic process
D0006527biological_processarginine catabolic process
D0016787molecular_functionhydrolase activity
D0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
D0019547biological_processarginine catabolic process to ornithine
D0030145molecular_functionmanganese ion binding
D0035578cellular_componentazurophil granule lumen
D0035580cellular_componentspecific granule lumen
D0042130biological_processnegative regulation of T cell proliferation
D0042832biological_processdefense response to protozoan
D0045087biological_processinnate immune response
D0046007biological_processnegative regulation of activated T cell proliferation
D0046872molecular_functionmetal ion binding
D0060336biological_processnegative regulation of type II interferon-mediated signaling pathway
D0070965biological_processpositive regulation of neutrophil mediated killing of fungus
D2000552biological_processnegative regulation of T-helper 2 cell cytokine production
E0000050biological_processurea cycle
E0002250biological_processadaptive immune response
E0004053molecular_functionarginase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006525biological_processarginine metabolic process
E0006527biological_processarginine catabolic process
E0016787molecular_functionhydrolase activity
E0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
E0019547biological_processarginine catabolic process to ornithine
E0030145molecular_functionmanganese ion binding
E0035578cellular_componentazurophil granule lumen
E0035580cellular_componentspecific granule lumen
E0042130biological_processnegative regulation of T cell proliferation
E0042832biological_processdefense response to protozoan
E0045087biological_processinnate immune response
E0046007biological_processnegative regulation of activated T cell proliferation
E0046872molecular_functionmetal ion binding
E0060336biological_processnegative regulation of type II interferon-mediated signaling pathway
E0070965biological_processpositive regulation of neutrophil mediated killing of fungus
E2000552biological_processnegative regulation of T-helper 2 cell cytokine production
F0000050biological_processurea cycle
F0002250biological_processadaptive immune response
F0004053molecular_functionarginase activity
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006525biological_processarginine metabolic process
F0006527biological_processarginine catabolic process
F0016787molecular_functionhydrolase activity
F0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
F0019547biological_processarginine catabolic process to ornithine
F0030145molecular_functionmanganese ion binding
F0035578cellular_componentazurophil granule lumen
F0035580cellular_componentspecific granule lumen
F0042130biological_processnegative regulation of T cell proliferation
F0042832biological_processdefense response to protozoan
F0045087biological_processinnate immune response
F0046007biological_processnegative regulation of activated T cell proliferation
F0046872molecular_functionmetal ion binding
F0060336biological_processnegative regulation of type II interferon-mediated signaling pathway
F0070965biological_processpositive regulation of neutrophil mediated killing of fungus
F2000552biological_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 1001
ChainResidue
AHIS101
AASP124
AASP128
AASP232
AMN1002
AQRA1003

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 1002
ChainResidue
AASP234
AMN1001
AQRA1003
AASP124
AHIS126
AASP232

site_idAC3
Number of Residues22
Detailsbinding site for residue QRA A 1003
ChainResidue
AHIS101
AASP124
AHIS126
AASP128
AASN130
ASER137
AHIS141
AASP181
AASP183
AGLU186
AASP232
AASP234
ATHR246
AGLU277
AMN1001
AMN1002
AHOH1105
AHOH1106
AHOH1114
AHOH1177
AHOH1183
AHOH1192

site_idAC4
Number of Residues6
Detailsbinding site for residue MN B 1001
ChainResidue
BHIS101
BASP124
BASP128
BASP232
BMN1002
BQRA1003

site_idAC5
Number of Residues6
Detailsbinding site for residue MN B 1002
ChainResidue
BASP124
BHIS126
BASP232
BASP234
BMN1001
BQRA1003

site_idAC6
Number of Residues20
Detailsbinding site for residue QRA B 1003
ChainResidue
BHIS101
BASP124
BHIS126
BASP128
BASN130
BSER137
BHIS141
BASP183
BGLU186
BASP232
BASP234
BTHR246
BGLU277
BMN1001
BMN1002
BHOH1111
BHOH1119
BHOH1160
BHOH1165
BHOH1177

site_idAC7
Number of Residues6
Detailsbinding site for residue MN C 1001
ChainResidue
CHIS101
CASP124
CASP128
CASP232
CMN1002
CQRA1003

site_idAC8
Number of Residues6
Detailsbinding site for residue MN C 1002
ChainResidue
CASP124
CHIS126
CASP232
CASP234
CMN1001
CQRA1003

site_idAC9
Number of Residues21
Detailsbinding site for residue QRA C 1003
ChainResidue
CHIS101
CASP124
CHIS126
CASP128
CASN130
CSER137
CHIS141
CASP181
CASP183
CGLU186
CASP232
CASP234
CTHR246
CGLU277
CMN1001
CMN1002
CHOH1104
CHOH1108
CHOH1130
CHOH1156
CHOH1162

site_idAD1
Number of Residues6
Detailsbinding site for residue MN D 1001
ChainResidue
DHIS101
DASP124
DASP128
DASP232
DMN1002
DQRA1003

site_idAD2
Number of Residues6
Detailsbinding site for residue MN D 1002
ChainResidue
DASP124
DHIS126
DASP232
DASP234
DMN1001
DQRA1003

site_idAD3
Number of Residues21
Detailsbinding site for residue QRA D 1003
ChainResidue
DHIS101
DASP124
DHIS126
DASP128
DASN130
DSER137
DHIS141
DASP183
DGLU186
DASP232
DASP234
DTHR246
DGLU277
DMN1001
DMN1002
DHOH1102
DHOH1103
DHOH1127
DHOH1143
DHOH1153
DHOH1172

site_idAD4
Number of Residues6
Detailsbinding site for residue MN E 1001
ChainResidue
EHIS101
EASP124
EASP128
EASP232
EMN1002
EQRA1003

site_idAD5
Number of Residues6
Detailsbinding site for residue MN E 1002
ChainResidue
EASP124
EHIS126
EASP232
EASP234
EMN1001
EQRA1003

site_idAD6
Number of Residues20
Detailsbinding site for residue QRA E 1003
ChainResidue
EHIS101
EASP124
EHIS126
EASP128
EASN130
ESER137
EHIS141
EASP181
EASP183
EGLU186
EASP232
EASP234
ETHR246
EGLU277
EMN1001
EMN1002
EHOH1104
EHOH1120
EHOH1126
EHOH1158

site_idAD7
Number of Residues6
Detailsbinding site for residue MN F 1001
ChainResidue
FHIS101
FASP124
FASP128
FASP232
FMN1002
FQRA1003

site_idAD8
Number of Residues6
Detailsbinding site for residue MN F 1002
ChainResidue
FASP124
FHIS126
FASP232
FASP234
FMN1001
FQRA1003

site_idAD9
Number of Residues21
Detailsbinding site for residue QRA F 1003
ChainResidue
FHIS101
FASP124
FHIS126
FASP128
FASN130
FSER137
FHIS141
FASP181
FASP183
FGLU186
FASP232
FASP234
FTHR246
FGLU277
FMN1001
FMN1002
FHOH1105
FHOH1107
FHOH1128
FHOH1136
FHOH1184

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 Residues36
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
CHIS101
CASP124
CHIS126
CASP128
CASP232
CASP234
DHIS101
AASP124
DASP124
DHIS126
DASP128
DASP232
DASP234
EHIS101
EASP124
EHIS126
EASP128
EASP232
AHIS126
EASP234
FHIS101
FASP124
FHIS126
FASP128
FASP232
FASP234
AASP128
AASP232
AASP234
BHIS101
BASP124
BHIS126

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0, ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3THJ
ChainResidueDetails
ASER137
EASP183
FSER137
FASP183
AASP183
BSER137
BASP183
CSER137
CASP183
DSER137
DASP183
ESER137

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P53608
ChainResidueDetails
ATHR246
BTHR246
CTHR246
DTHR246
ETHR246
FTHR246

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P78540
ChainResidueDetails
AGLU277
BGLU277
CGLU277
DGLU277
EGLU277
FGLU277

site_idSWS_FT_FI5
Number of Residues12
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q61176
ChainResidueDetails
ALYS17
ELYS75
FLYS17
FLYS75
ALYS75
BLYS17
BLYS75
CLYS17
CLYS75
DLYS17
DLYS75
ELYS17

site_idSWS_FT_FI6
Number of Residues18
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER62
DSER62
DSER163
DSER217
ESER62
ESER163
ESER217
FSER62
FSER163
FSER217
ASER163
ASER217
BSER62
BSER163
BSER217
CSER62
CSER163
CSER217

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q61176
ChainResidueDetails
ASER72
BSER72
CSER72
DSER72
ESER72
FSER72

219140

PDB entries from 2024-05-01

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