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4Q3S

Crystal structure of Schistosoma mansoni arginase in complex with inhibitor ABHPE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0004053molecular_functionarginase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006525biological_processarginine metabolic 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
A0046872molecular_functionmetal ion binding
B0000050biological_processurea cycle
B0004053molecular_functionarginase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006525biological_processarginine metabolic 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
B0046872molecular_functionmetal ion binding
C0000050biological_processurea cycle
C0004053molecular_functionarginase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006525biological_processarginine metabolic 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
C0046872molecular_functionmetal ion binding
D0000050biological_processurea cycle
D0004053molecular_functionarginase activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006525biological_processarginine metabolic 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
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AHIS131
AASP154
AASP158
AASP262
AMN402
AX7A403

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AASP264
AMN401
AX7A403
AASP154
AHIS156
AASP262

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE X7A A 403
ChainResidue
AHIS131
AASP154
AHIS156
AASP158
AASN160
ASER167
AHIS171
AASP211
AASP213
AASP262
AASP264
ATHR276
AGLU307
AMN401
AMN402
AHOH501
AHOH502
AHOH503
AHOH504
AHOH512

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
AASP79
APRO80
AGLN81
ALYS86
ATRP87

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
AASN32
AGLU73
AHOH721

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 406
ChainResidue
ATYR227
AASP232
AHOH613

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
BHIS131
BASP154
BASP158
BASP262
BMN402
BX7A403

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 402
ChainResidue
BASP154
BHIS156
BASP262
BASP264
BMN401
BX7A403

site_idAC9
Number of Residues21
DetailsBINDING SITE FOR RESIDUE X7A B 403
ChainResidue
BHIS131
BASP154
BHIS156
BASP158
BASN160
BSER167
BHIS171
BASP211
BASP213
BASP262
BASP264
BTHR276
BGLU307
BMN401
BMN402
BHOH501
BHOH502
BHOH506
BHOH507
BHOH549
BHOH557

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 404
ChainResidue
BASP79
BPRO80
BGLN81
BLYS86
BTRP87

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 405
ChainResidue
BASN32
BILE38
BGLU73
BHOH540

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 406
ChainResidue
BTYR227
BASP232

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 401
ChainResidue
CHIS131
CASP154
CASP158
CASP262
CMN402
CX7A403

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 402
ChainResidue
CASP154
CHIS156
CASP262
CASP264
CMN401
CX7A403

site_idBC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE X7A C 403
ChainResidue
CHIS131
CASP154
CHIS156
CASP158
CASN160
CSER167
CHIS171
CASP211
CASP213
CASP262
CASP264
CTHR276
CGLU307
CMN401
CMN402
CHOH502
CHOH503
CHOH504
CHOH531

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 404
ChainResidue
CASP79
CPRO80
CGLN81
CLYS86
CTRP87

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 405
ChainResidue
CASN32
CILE38
CGLU73
CHOH568

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN D 401
ChainResidue
DHIS131
DASP154
DASP158
DASP262
DMN402
DX7A403

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN D 402
ChainResidue
DASP154
DHIS156
DASP262
DASP264
DMN401
DX7A403

site_idCC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE X7A D 403
ChainResidue
DHIS131
DASP154
DHIS156
DASP158
DASN160
DSER167
DHIS171
DASP211
DASP213
DASP262
DASP264
DTHR276
DGLU307
DMN401
DMN402
DHOH501
DHOH508
DHOH511
DHOH522

Functional Information from PROSITE/UniProt
site_idPS01053
Number of Residues22
DetailsARGINASE_1 Arginase family signature. SFDIDaldPlvaPStgtavpgG
ChainResidueDetails
ASER260-GLY281

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PDB entries from 2024-07-31

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