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3BPM

Crystal Structure of Falcipain-3 with Its inhibitor, Leupeptin

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ALYS20
AALA24
ALYS25
ALEU26
AARG28

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AALA24
ALYS25
AARG150
AHOH419

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AARG202
BARG28

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
AARG202
BLYS20
BLYS25
BLEU26
BARG28

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BARG150

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR CHAIN C OF LEUPEPTIN
ChainResidue
BGLN45
BGLY49
BSER50
BCYS51
BTRP52
BTYR90
BGLY91
BGLY92
BTYR93
BASN182
BHIS183

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR CHAIN D OF LEUPEPTIN
ChainResidue
AGLN45
AGLY49
ASER50
ACYS51
ATRP52
ATYR90
AGLY91
AGLY92
ATYR93
AASP164
AGLU176
AASN182
AHIS183
AHOH405
AHOH408
DHOH101
DHOH102
DHOH103

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QAlCGSCWAfSS
ChainResidueDetails
AGLN45-SER56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088
ChainResidueDetails
ACYS51
BCYS51

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089
ChainResidueDetails
AHIS183
BHIS183

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090
ChainResidueDetails
AASN213
BASN213

220113

PDB entries from 2024-05-22

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