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6DKT

Crystal structure of Arginase from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0004053molecular_functionarginase activity
A0005737cellular_componentcytoplasm
A0006525biological_processarginine metabolic process
A0016787molecular_functionhydrolase activity
A0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
B0000050biological_processurea cycle
B0004053molecular_functionarginase activity
B0005737cellular_componentcytoplasm
B0006525biological_processarginine metabolic process
B0016787molecular_functionhydrolase activity
B0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
C0000050biological_processurea cycle
C0004053molecular_functionarginase activity
C0005737cellular_componentcytoplasm
C0006525biological_processarginine metabolic process
C0016787molecular_functionhydrolase activity
C0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
C0030145molecular_functionmanganese ion binding
C0046872molecular_functionmetal ion binding
D0000050biological_processurea cycle
D0004053molecular_functionarginase activity
D0005737cellular_componentcytoplasm
D0006525biological_processarginine metabolic process
D0016787molecular_functionhydrolase activity
D0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
D0030145molecular_functionmanganese ion binding
D0046872molecular_functionmetal ion binding
E0000050biological_processurea cycle
E0004053molecular_functionarginase activity
E0005737cellular_componentcytoplasm
E0006525biological_processarginine metabolic process
E0016787molecular_functionhydrolase activity
E0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
E0030145molecular_functionmanganese ion binding
E0046872molecular_functionmetal ion binding
F0000050biological_processurea cycle
F0004053molecular_functionarginase activity
F0005737cellular_componentcytoplasm
F0006525biological_processarginine metabolic process
F0016787molecular_functionhydrolase activity
F0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
F0030145molecular_functionmanganese ion binding
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MN A 500
ChainResidue
AHIS97
AASP120
AASP124
AASP223
AMN501
AHOH643
AHOH659

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 501
ChainResidue
AASP223
AASP225
AMN500
AHOH643
AASP120
AHIS122

site_idAC3
Number of Residues6
Detailsbinding site for residue MN B 500
ChainResidue
BHIS97
BTRP118
BASP120
BASP124
BASP223
BMN501

site_idAC4
Number of Residues5
Detailsbinding site for residue MN B 501
ChainResidue
BASP120
BHIS122
BASP223
BASP225
BMN500

site_idAC5
Number of Residues5
Detailsbinding site for residue MN C 500
ChainResidue
CHIS97
CASP120
CASP124
CASP223
CMN501

site_idAC6
Number of Residues5
Detailsbinding site for residue MN C 501
ChainResidue
CASP120
CHIS122
CASP223
CASP225
CMN500

site_idAC7
Number of Residues7
Detailsbinding site for residue MN D 500
ChainResidue
DHIS97
DTRP118
DASP120
DASP124
DASP223
DMN501
DHOH688

site_idAC8
Number of Residues5
Detailsbinding site for residue MN D 501
ChainResidue
DASP120
DHIS122
DASP223
DASP225
DMN500

site_idAC9
Number of Residues7
Detailsbinding site for residue MN E 500
ChainResidue
EHIS97
ETRP118
EASP120
EASP124
EASP223
EMN501
EHOH633

site_idAD1
Number of Residues6
Detailsbinding site for residue MN E 501
ChainResidue
EASP120
EHIS122
EASP223
EASP225
EMN500
EHOH633

site_idAD2
Number of Residues6
Detailsbinding site for residue MN F 500
ChainResidue
FHIS97
FASP120
FASP124
FASP223
FMN501
FHOH610

site_idAD3
Number of Residues6
Detailsbinding site for residue MN F 501
ChainResidue
FASP120
FHIS122
FASP223
FASP225
FMN500
FHOH610

Functional Information from PROSITE/UniProt
site_idPS01053
Number of Residues22
DetailsARGINASE_1 Arginase family signature. SLDLDgldPndaPGvgtpvvgG
ChainResidueDetails
ASER221-GLY242

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00742","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues52
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P53608","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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