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

4Q3U

Crystal structure of Schistosoma mansoni arginase in complex with inhibitor nor-NOHA

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
ANNH405

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AASP264
AMN401
ANNH405
AASP154
AHIS156
AASP262

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AASP79
APRO80
AGLN81
ALYS86
ATRP87

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
AASN32
ATYR41
AGLU73
AHOH627

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NNH A 405
ChainResidue
AASP154
AHIS156
AASP158
AASN160
ASER167
AHIS171
AGLY172
AASP213
AASP262
AASP264
ATHR276
AMN401
AMN402
AHOH504
AHOH524
AHOH619

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
BHIS131
BASP154
BASP158
BASP262
BMN402
BNNH405

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 402
ChainResidue
BASP154
BHIS156
BASP262
BASP264
BMN401
BNNH405

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 403
ChainResidue
BASP79
BGLN81
BLYS86
BTRP87

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 404
ChainResidue
BASN32
BILE38
BGLU73
BHOH621

site_idBC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NNH B 405
ChainResidue
BASP154
BHIS156
BASP158
BASN160
BSER167
BHIS171
BGLY172
BASP213
BASP262
BASP264
BTHR276
BMN401
BMN402
BHOH510
BHOH535
BHOH537
BHOH617

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 401
ChainResidue
CHIS131
CASP154
CASP158
CASP262
CMN402
CNNH405

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 402
ChainResidue
CASP154
CHIS156
CASP262
CASP264
CMN401
CNNH405

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 403
ChainResidue
CASP79
CPRO80
CGLN81
CLYS86
CTRP87

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL C 404
ChainResidue
CASN32
CILE38
CGLU73

site_idBC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NNH C 405
ChainResidue
CHIS171
CGLY172
CASP213
CASP262
CASP264
CTHR276
CMN401
CMN402
CHOH531
CHOH540
CHOH563
CASP154
CHIS156
CASP158
CASN160
CSER167

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN D 401
ChainResidue
DHIS131
DASP154
DASP158
DASP262
DMN402
DNNH403

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN D 402
ChainResidue
DASP154
DHIS156
DASP262
DASP264
DMN401
DNNH403

site_idBC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NNH D 403
ChainResidue
DASP154
DHIS156
DASP158
DASN160
DSER167
DHIS171
DGLY172
DASP213
DGLU216
DASP262
DASP264
DTHR276
DMN401
DMN402

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

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon