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5ZEH

Crystal structure of Entamoeba histolytica Arginase in complex with L- Ornithine at 2.35 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000050biological_processurea cycle
A0004053molecular_functionarginase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006525biological_processarginine metabolic process
A0016787molecular_functionhydrolase activity
A0019547biological_processarginine catabolic process to ornithine
A0030145molecular_functionmanganese ion binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0000050biological_processurea cycle
B0004053molecular_functionarginase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006525biological_processarginine metabolic process
B0016787molecular_functionhydrolase activity
B0019547biological_processarginine catabolic process to ornithine
B0030145molecular_functionmanganese ion binding
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue ORN A 301
ChainResidue
AHIS126
AASP128
AASN130
ASER137
AHIS141
AASP178
AHOH401
AHOH403
AHOH406

site_idAC2
Number of Residues7
Detailsbinding site for residue MN A 302
ChainResidue
AHIS98
AASP124
AASP128
AASP225
AMN303
AHOH401
AHOH406

site_idAC3
Number of Residues6
Detailsbinding site for residue MN A 303
ChainResidue
AASP124
AHIS126
AASP225
AASP227
AMN302
AHOH401

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 304
ChainResidue
AASN115
AARG117
AASP218

site_idAC5
Number of Residues10
Detailsbinding site for residue ORN B 301
ChainResidue
BHIS126
BASP128
BASN130
BSER137
BHIS141
BGLY142
BASP178
BHOH402
BHOH405
BHOH412

site_idAC6
Number of Residues6
Detailsbinding site for residue MN B 302
ChainResidue
BHIS98
BASP124
BASP128
BASP225
BMN303
BHOH402

site_idAC7
Number of Residues6
Detailsbinding site for residue MN B 303
ChainResidue
BASP124
BHIS126
BASP225
BASP227
BMN302
BHOH402

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:31199070, ECO:0007744|PDB:5ZEE, ECO:0007744|PDB:5ZEF, ECO:0007744|PDB:5ZEH
ChainResidueDetails
AHIS98
BASP128
BASP225
BASP227
AASP124
AHIS126
AASP128
AASP225
AASP227
BHIS98
BASP124
BHIS126

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:31199070, ECO:0007744|PDB:5ZEE, ECO:0007744|PDB:5ZEF, ECO:0007744|PDB:5ZEH
ChainResidueDetails
AASN130
ASER137
AASP178
ATHR239
BASN130
BSER137
BASP178
BTHR239

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PDB entries from 2024-10-30

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