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3SL0

Crystal Structure of P. falciparum arginase complexed with 2-amino-6-borono-2-(difluoromethyl)hexanoic acid

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 412
ChainResidue
AASP216
AHIS218
AASP323
AASP325
AMN413
AFB5414

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 413
ChainResidue
AASP323
AMN412
AFB5414
AHOH598
AHIS193
AASP216
AASP220

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FB5 A 414
ChainResidue
AASP216
AHIS218
AASP220
AASN222
ASER229
AHIS233
AGLY234
AASP274
AASP323
AASP325
AGLU368
AHIS381
AMN412
AMN413
AHOH436
AHOH479
AHOH508
AHOH511
AHOH598

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20527960, ECO:0000269|PubMed:21728378, ECO:0007744|PDB:3MMR, ECO:0007744|PDB:3SL0, ECO:0007744|PDB:3SL1
ChainResidueDetails
AHIS193
AASP216
AHIS218
AASP220
AASP323
AASP325

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:20527960, ECO:0000305|PubMed:21728378, ECO:0007744|PDB:3MMR, ECO:0007744|PDB:3SL0, ECO:0007744|PDB:3SL1
ChainResidueDetails
AASN222
ASER229
AASP274

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PDB entries from 2024-06-26

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