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4CKU

Three dimensional structure of plasmepsin II in complex with hydroxyethylamine-based inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
E0004190molecular_functionaspartic-type endopeptidase activity
E0006508biological_processproteolysis
F0004190molecular_functionaspartic-type endopeptidase activity
F0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE P2F A 400
ChainResidue
AILE14
AGLY216
ATHR217
ASER218
AILE300
AHOH2059
AHOH2060
AHOH2182
AHOH2183
AILE32
AASP34
AGLY36
ATYR77
AVAL78
ASER79
ATYR192
AASP214

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE P2F B 400
ChainResidue
BILE14
BILE32
BASP34
BGLY36
BVAL78
BSER79
BPHE111
BILE123
BTYR192
BASP214
BGLY216
BTHR217
BSER218
BILE290
BLEU292
BPHE294
BILE300
BHOH2081
BHOH2218

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE P2F C 400
ChainResidue
CMET15
CILE32
CASP34
CGLY36
CVAL78
CPHE111
CTYR192
CASP214
CGLY216
CTHR217
CSER218
CILE290
CLEU292
CILE300
CHOH2085

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE P2F D 400
ChainResidue
DMET15
DILE32
DASP34
DGLY36
DVAL78
DSER79
DPHE111
DTHR114
DTYR192
DASP214
DGLY216
DTHR217
DSER218
DILE300
DHOH2086

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE P2F E 400
ChainResidue
EMET15
EILE32
EASP34
EGLY36
ETYR77
EVAL78
ESER79
EPHE111
EILE123
ETYR192
EASP214
EGLY216
ETHR217
ESER218
EILE290
EILE300
EHOH2073
EHOH2182

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE P2F F 400
ChainResidue
FHOH2193
FMET15
FILE32
FASP34
FGLY36
FSER37
FVAL78
FSER79
FPHE111
FTYR192
FASP214
FGLY216
FTHR217
FSER218
FLEU292
FHOH2073

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. FILDTGSANLWV
ChainResidueDetails
APHE31-VAL42
ACYS211-VAL222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP34
EASP214
FASP34
FASP214
AASP214
BASP34
BASP214
CASP34
CASP214
DASP34
DASP214
EASP34

222415

PDB entries from 2024-07-10

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