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5ZEF

Crystal structure of Entamoeba histolytica Arginase in complex with L- Norvaline at 2.01 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 Residues8
Detailsbinding site for residue NVA A 301
ChainResidue
AASN130
ASER137
AHIS141
AASP178
AHOH403
AHOH413
AHOH421
AHOH463

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 302
ChainResidue
AASP124
AASP128
AASP225
AMN303
AHOH426
AHIS98

site_idAC3
Number of Residues7
Detailsbinding site for residue MN A 303
ChainResidue
AASP124
AHIS126
AASP225
AASP227
AMN302
AHOH426
AHOH463

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 304
ChainResidue
AMET160
APRO161
AHIS162
ATYR163
AHOH401
AHOH460

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 305
ChainResidue
AILE50
ATHR51
APRO53
ASER72
AVAL73
AGLU76

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 306
ChainResidue
AVAL109
ALYS110
AMET112
BSER158
BEDO304

site_idAC7
Number of Residues6
Detailsbinding site for residue NVA B 301
ChainResidue
BHIS126
BASN130
BSER137
BHIS141
BASP178
BHOH410

site_idAC8
Number of Residues6
Detailsbinding site for residue MN B 302
ChainResidue
BHIS98
BASP124
BASP128
BASP225
BMN303
BHOH431

site_idAC9
Number of Residues7
Detailsbinding site for residue MN B 303
ChainResidue
BASP124
BHIS126
BASP225
BASP227
BMN302
BHOH431
BHOH437

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO B 304
ChainResidue
ALYS110
AALA111
AEDO306
BARG78
BSER158
BHOH419

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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