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3MMR

Structure of Plasmodium falciparum Arginase in complex with ABH

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
AHIS193
AASP216
AASP220
AASP323
AMN413
AABH551

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 413
ChainResidue
AASP325
AMN412
AABH551
AASP216
AHIS218
AASP323

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ABH A 551
ChainResidue
AHIS193
AASP216
AHIS218
AASP220
AASN222
ASER229
AHIS233
AASP274
AGLU277
AASP323
AASP325
AGLU368
AHIS381
AMN412
AMN413
AHOH424
AHOH445
AHOH475
AHOH525

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BME A 414
ChainResidue
AASP328
APHE331
AGLY341
AASN344
ATYR345
AARG346
AHOH435
AHOH545

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 2024-07-31

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