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3kqz

Structure of a protease 2

Method: X-RAY DIFFRACTION Dmax: 215.2 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

M17 leucyl aminopeptidase

Plasmodium falciparum

UniProt Q8IL11

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count Chain A； UniProt 84–605 Chain B； UniProt 84–605 Chain C； UniProt 84–605 Chain D； UniProt 84–605 Chain E； UniProt 84–605 Chain F； UniProt 84–605 Fragment：residues 84-605 Mutation：N152Q, N515Q, N546Q CO3 CARBONATE ION × 6 ZN ZINC ION × 12 SO4 SULFATE ION × 16 1PE PENTAETHYLENE GLYCOL × 24 2PE NONAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris pH 8.5, 0.2M LiSO4, 1mM TCEP, 1mM ZnCl2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.39 Å R-free 0.242
2 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count Chain G； UniProt 84–605 Chain H； UniProt 84–605 Chain I； UniProt 84–605 Chain J； UniProt 84–605 Chain K； UniProt 84–605 Chain L； UniProt 84–605 Fragment：residues 84-605 Mutation：N152Q, N515Q, N546Q CO3 CARBONATE ION × 6 ZN ZINC ION × 12 SO4 SULFATE ION × 11 1PE PENTAETHYLENE GLYCOL × 29 2PE NONAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris pH 8.5, 0.2M LiSO4, 1mM TCEP, 1mM ZnCl2, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.39 Å R-free 0.242

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 3KQZ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3KQX Structure of a protease 1 Deposited 2009-11-17 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 84–605（522 aa） Fragment：residues 84-605
Chain B 84–605（522 aa） Fragment：residues 84-605
Chain C 84–605（522 aa） Fragment：residues 84-605
Chain D 84–605（522 aa） Fragment：residues 84-605
Chain E 84–605（522 aa） Fragment：residues 84-605
Chain F 84–605（522 aa） Fragment：residues 84-605
Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q ZN ZINC ION × 6 CO3 CARBONATE ION × 6 SO4 SULFATE ION × 11 1PE PENTAETHYLENE GLYCOL × 24 2PE NONAETHYLENE GLYCOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris pH 8.5, 0.2M LiSO4, 1mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.01 Å R-free 0.232
3KQX Structure of a protease 1 Deposited 2009-11-17 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 84–605（522 aa） Fragment：residues 84-605
Chain H 84–605（522 aa） Fragment：residues 84-605
Chain I 84–605（522 aa） Fragment：residues 84-605
Chain J 84–605（522 aa） Fragment：residues 84-605
Chain K 84–605（522 aa） Fragment：residues 84-605
Chain L 84–605（522 aa） Fragment：residues 84-605
Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q ZN ZINC ION × 6 CO3 CARBONATE ION × 6 SO4 SULFATE ION × 5 1PE PENTAETHYLENE GLYCOL × 30 2PE NONAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris pH 8.5, 0.2M LiSO4, 1mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.01 Å R-free 0.232
3KR4 Structure of a protease 3 Deposited 2009-11-17 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 84–605（522 aa） Fragment：residues 84-605
Chain B 84–605（522 aa） Fragment：residues 84-605
Chain C 84–605（522 aa） Fragment：residues 84-605
Chain D 84–605（522 aa） Fragment：residues 84-605
Chain E 84–605（522 aa） Fragment：residues 84-605
Chain F 84–605（522 aa） Fragment：residues 84-605
Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q CO3 CARBONATE ION × 6 ZN ZINC ION × 6 BES 2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC ACID × 6 MG MAGNESIUM ION × 6 SO4 SULFATE ION × 8 1PE PENTAETHYLENE GLYCOL × 17 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris pH 8.5, 0.2M LiSo4, 1mM TCEP, 1mM MgCl2, 1mM Bestatin, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.242
3KR4 Structure of a protease 3 Deposited 2009-11-17 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 84–605（522 aa） Fragment：residues 84-605
Chain H 84–605（522 aa） Fragment：residues 84-605
Chain I 84–605（522 aa） Fragment：residues 84-605
Chain J 84–605（522 aa） Fragment：residues 84-605
Chain K 84–605（522 aa） Fragment：residues 84-605
Chain L 84–605（522 aa） Fragment：residues 84-605
Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q CO3 CARBONATE ION × 6 ZN ZINC ION × 6 BES 2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC ACID × 6 MG MAGNESIUM ION × 6 SO4 SULFATE ION × 6 1PE PENTAETHYLENE GLYCOL × 20 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris pH 8.5, 0.2M LiSo4, 1mM TCEP, 1mM MgCl2, 1mM Bestatin, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.242
3KR5 Structure of a protease 4 Deposited 2009-11-17 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 84–605（522 aa） Fragment：residues 84-605
Chain B 84–605（522 aa） Fragment：residues 84-605
Chain C 84–605（522 aa） Fragment：residues 84-605
Chain D 84–605（522 aa） Fragment：residues 84-605
Chain E 84–605（522 aa） Fragment：residues 84-605
Chain F 84–605（522 aa） Fragment：residues 84-605
Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q CO3 CARBONATE ION × 6 ZN ZINC ION × 12 BEY (2S)-3-[(R)-[(1S)-1-amino-3-phenylpropyl](hydroxy)phosphoryl]-2-benzylpropanoic acid × 6 SO4 SULFATE ION × 8 1PE PENTAETHYLENE GLYCOL × 17 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris pH 8.5, 0.2M LiSO4, 1mM TCEP, 1mM ZnCl2, 1mM Co4/BEY, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.56 Å R-free 0.278
3KR5 Structure of a protease 4 Deposited 2009-11-17 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 84–605（522 aa） Fragment：residues 84-605
Chain H 84–605（522 aa） Fragment：residues 84-605
Chain I 84–605（522 aa） Fragment：residues 84-605
Chain J 84–605（522 aa） Fragment：residues 84-605
Chain K 84–605（522 aa） Fragment：residues 84-605
Chain L 84–605（522 aa） Fragment：residues 84-605
Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q CO3 CARBONATE ION × 6 ZN ZINC ION × 12 BEY (2S)-3-[(R)-[(1S)-1-amino-3-phenylpropyl](hydroxy)phosphoryl]-2-benzylpropanoic acid × 6 SO4 SULFATE ION × 7 1PE PENTAETHYLENE GLYCOL × 20 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris pH 8.5, 0.2M LiSO4, 1mM TCEP, 1mM ZnCl2, 1mM Co4/BEY, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.56 Å R-free 0.278
3T8W A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases Deposited 2011-08-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 84–605（522 aa） Fragment：UNP residues 84-605
Chain B 84–605（522 aa） Fragment：UNP residues 84-605
Chain C 84–605（522 aa） Fragment：UNP residues 84-605
Chain D 84–605（522 aa） Fragment：UNP residues 84-605
Chain E 84–605（522 aa） Fragment：UNP residues 84-605
Chain F 84–605（522 aa） Fragment：UNP residues 84-605
Not recorded CO3 CARBONATE ION × 6 ZN ZINC ION × 12 DGZ N-((2R,3S,6S,18S,21S)-2-amino-18-(4-benzoylbenzyl)-21-carbamoyl-3-hydroxy-6-(naphthalen-2-ylmethyl)-4,7,16,19-tetraoxo-1-phenyl-11,14-dioxa-5,8,17,20-tetraazapentacosan-25-yl)hex-5-ynamide × 6 SO4 SULFATE ION × 12 1PE PENTAETHYLENE GLYCOL × 14 2PE NONAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40%(v/v) PEG400, 0.1M Tris, 0.2M LiSO4, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.200
3T8W A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases Deposited 2011-08-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 84–605（522 aa） Fragment：UNP residues 84-605
Chain H 84–605（522 aa） Fragment：UNP residues 84-605
Chain I 84–605（522 aa） Fragment：UNP residues 84-605
Chain J 84–605（522 aa） Fragment：UNP residues 84-605
Chain K 84–605（522 aa） Fragment：UNP residues 84-605
Chain L 84–605（522 aa） Fragment：UNP residues 84-605
Not recorded CO3 CARBONATE ION × 6 ZN ZINC ION × 12 DGZ N-((2R,3S,6S,18S,21S)-2-amino-18-(4-benzoylbenzyl)-21-carbamoyl-3-hydroxy-6-(naphthalen-2-ylmethyl)-4,7,16,19-tetraoxo-1-phenyl-11,14-dioxa-5,8,17,20-tetraazapentacosan-25-yl)hex-5-ynamide × 6 SO4 SULFATE ION × 17 1PE PENTAETHYLENE GLYCOL × 19 2PE NONAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40%(v/v) PEG400, 0.1M Tris, 0.2M LiSO4, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.200
4K3N Phosphonic Arginine Mimetics as Inhibitors of the M17 Aminopeptidases from Plasmodium falciparum Deposited 2013-04-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 84–605（522 aa） Fragment：unp residues 84-605
Chain B 84–605（522 aa） Fragment：unp residues 84-605
Chain C 84–605（522 aa） Fragment：unp residues 84-605
Chain D 84–605（522 aa） Fragment：unp residues 84-605
Chain E 84–605（522 aa） Fragment：unp residues 84-605
Chain F 84–605（522 aa） Fragment：unp residues 84-605
Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N ZN ZINC ION × 12 CO3 CARBONATE ION × 6 1OT {(R)-amino[4-(1H-pyrazol-1-yl)phenyl]methyl}phosphonic acid × 6 SO4 SULFATE ION × 11 1PE PENTAETHYLENE GLYCOL × 15 2PE NONAETHYLENE GLYCOL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris, 0.2M LiSO4, 1mM TCEP, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.240
4K3N Phosphonic Arginine Mimetics as Inhibitors of the M17 Aminopeptidases from Plasmodium falciparum Deposited 2013-04-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 84–605（522 aa） Fragment：unp residues 84-605
Chain H 84–605（522 aa） Fragment：unp residues 84-605
Chain I 84–605（522 aa） Fragment：unp residues 84-605
Chain J 84–605（522 aa） Fragment：unp residues 84-605
Chain K 84–605（522 aa） Fragment：unp residues 84-605
Chain L 84–605（522 aa） Fragment：unp residues 84-605
Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N ZN ZINC ION × 12 CO3 CARBONATE ION × 6 1OT {(R)-amino[4-(1H-pyrazol-1-yl)phenyl]methyl}phosphonic acid × 6 SO4 SULFATE ION × 10 1PE PENTAETHYLENE GLYCOL × 19 2PE NONAETHYLENE GLYCOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% PEG 400, 0.1M Tris, 0.2M LiSO4, 1mM TCEP, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.240
4R6T Structure of the m17 leucyl aminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor Deposited 2014-08-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 84–605（522 aa）
Chain B 84–605（522 aa）
Chain C 84–605（522 aa）
Chain D 84–605（522 aa）
Chain E 84–605（522 aa）
Chain F 84–605（522 aa）
Not recorded ZN ZINC ION × 12 CO3 CARBONATE ION × 6 SO4 SULFATE ION × 12 R5T tert-butyl {(1S)-2-(hydroxyamino)-2-oxo-1-[4-(1H-pyrazol-1-yl)phenyl]ethyl}carbamate × 6 1PE PENTAETHYLENE GLYCOL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% (v/v) PEG 400, 0.1 M Tris pH 8.5, 0.2 M Li2SO4, 1 mM TCEP, vapor diffusion, hanging drop, temperature 298K
Resolution 2.60 Å R-free 0.269
4R6T Structure of the m17 leucyl aminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor Deposited 2014-08-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 84–605（522 aa）
Chain H 84–605（522 aa）
Chain I 84–605（522 aa）
Chain J 84–605（522 aa）
Chain K 84–605（522 aa）
Chain L 84–605（522 aa）
Not recorded ZN ZINC ION × 12 CO3 CARBONATE ION × 6 SO4 SULFATE ION × 11 R5T tert-butyl {(1S)-2-(hydroxyamino)-2-oxo-1-[4-(1H-pyrazol-1-yl)phenyl]ethyl}carbamate × 6 1PE PENTAETHYLENE GLYCOL × 8 DMS DIMETHYL SULFOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% (v/v) PEG 400, 0.1 M Tris pH 8.5, 0.2 M Li2SO4, 1 mM TCEP, vapor diffusion, hanging drop, temperature 298K
Resolution 2.60 Å R-free 0.269
4R7M Structure of the m17 leucyl aminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor Deposited 2014-08-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 84–605（522 aa） Fragment：unp residues 84-605
Chain B 84–605（522 aa） Fragment：unp residues 84-605
Chain C 84–605（522 aa） Fragment：unp residues 84-605
Chain D 84–605（522 aa） Fragment：unp residues 84-605
Chain E 84–605（522 aa） Fragment：unp residues 84-605
Chain F 84–605（522 aa） Fragment：unp residues 84-605
Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N ZN ZINC ION × 12 CO3 CARBONATE ION × 6 1PE PENTAETHYLENE GLYCOL × 7 3MW 4-amino-N-{(1R)-2-(hydroxyamino)-2-oxo-1-[4-(1H-pyrazol-1-yl)phenyl]ethyl}benzamide × 6 SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% (v/v) PEG 400, 0.1 M Tris pH 8.5, 0.2 M Li2SO4, 1 mM TCEP, vapor diffusion, hanging drop, temperature 298K
Resolution 2.85 Å R-free 0.291
4R7M Structure of the m17 leucyl aminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor Deposited 2014-08-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 84–605（522 aa） Fragment：unp residues 84-605
Chain H 84–605（522 aa） Fragment：unp residues 84-605
Chain I 84–605（522 aa） Fragment：unp residues 84-605
Chain J 84–605（522 aa） Fragment：unp residues 84-605
Chain K 84–605（522 aa） Fragment：unp residues 84-605
Chain L 84–605（522 aa） Fragment：unp residues 84-605
Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N Mutation：D152N, D515N, D516N ZN ZINC ION × 12 CO3 CARBONATE ION × 6 1PE PENTAETHYLENE GLYCOL × 4 3MW 4-amino-N-{(1R)-2-(hydroxyamino)-2-oxo-1-[4-(1H-pyrazol-1-yl)phenyl]ethyl}benzamide × 6 SO4 SULFATE ION × 5 DMS DIMETHYL SULFOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% (v/v) PEG 400, 0.1 M Tris pH 8.5, 0.2 M Li2SO4, 1 mM TCEP, vapor diffusion, hanging drop, temperature 298K
Resolution 2.85 Å R-free 0.291
4X2T X-ray crystal structure of the orally available aminopeptidase inhibitor, Tosedostat, bound to the M17 Leucyl Aminopeptidase from P. falciparum Deposited 2014-11-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain B 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain C 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain D 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain E 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain F 85–603（519 aa） Fragment：UNP residues 85 to 603
Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q ZN ZINC ION × 12 TOD (2S)-({(2R)-2-[(1S)-1-hydroxy-2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}amino)(phenyl)ethanoic acid × 5 CO3 CARBONATE ION × 6 SO4 SULFATE ION × 8 1PE PENTAETHYLENE GLYCOL × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.6；298 K；35% (v/v) PEG 400, 0.1 M Tris pH 8.6, 0.2 M Li2SO4
Resolution 2.73 Å R-free 0.274
4X2T X-ray crystal structure of the orally available aminopeptidase inhibitor, Tosedostat, bound to the M17 Leucyl Aminopeptidase from P. falciparum Deposited 2014-11-27 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain H 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain I 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain J 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain K 85–603（519 aa） Fragment：UNP residues 85 to 603
Chain L 85–603（519 aa） Fragment：UNP residues 85 to 603
Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q Mutation：N152Q, N515Q, N545Q ZN ZINC ION × 12 TOD (2S)-({(2R)-2-[(1S)-1-hydroxy-2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}amino)(phenyl)ethanoic acid × 6 CO3 CARBONATE ION × 6 SO4 SULFATE ION × 5 1PE PENTAETHYLENE GLYCOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.6；298 K；35% (v/v) PEG 400, 0.1 M Tris pH 8.6, 0.2 M Li2SO4
Resolution 2.73 Å R-free 0.274
7RIE Plasmodium falciparum M17 in complex with inhibitor MIPS2571 Deposited 2021-07-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 85–605（521 aa）
Chain B 85–605（521 aa）
Chain C 85–605（521 aa）
Chain D 85–605（521 aa）
Chain E 85–605（521 aa）
Chain F 85–605（521 aa）
Not recorded CO3 CARBONATE ION × 6 ZN ZINC ION × 12 1PE PENTAETHYLENE GLYCOL × 5 5IF N-{(1R)-2-(hydroxyamino)-1-[4'-(hydroxymethyl)[1,1'-biphenyl]-4-yl]-2-oxoethyl}-2,2-dimethylpropanamide × 6 SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG400, 0.2M LiSO4, 0.1M Tris pH 7.5 to 8.8
Resolution 2.49 Å R-free 0.229
7RIE Plasmodium falciparum M17 in complex with inhibitor MIPS2571 Deposited 2021-07-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 85–605（521 aa）
Chain H 85–605（521 aa）
Chain I 85–605（521 aa）
Chain J 85–605（521 aa）
Chain K 85–605（521 aa）
Chain L 85–605（521 aa）
Not recorded CO3 CARBONATE ION × 6 ZN ZINC ION × 12 1PE PENTAETHYLENE GLYCOL × 4 5IF N-{(1R)-2-(hydroxyamino)-1-[4'-(hydroxymethyl)[1,1'-biphenyl]-4-yl]-2-oxoethyl}-2,2-dimethylpropanamide × 6 SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG400, 0.2M LiSO4, 0.1M Tris pH 7.5 to 8.8
Resolution 2.49 Å R-free 0.229
7SRV Metal dependent activation of Plasmodium falciparum M17 aminopeptidase (inactive form), spacegroup P22121 Deposited 2021-11-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 85–605（521 aa）
Chain B 85–605（521 aa）
Chain C 85–605（521 aa）
Chain D 85–605（521 aa）
Chain E 85–605（521 aa）
Chain F 85–605（521 aa）
Not recorded ZN ZINC ION × 12 CO3 CARBONATE ION × 6 ACT ACETATE ION × 8 CA CALCIUM ION × 12 EDO 1,2-ETHANEDIOL × 6 PO4 PHOSPHATE ION × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；20 % PEG3350, 0.2 M calcium acetate
Resolution 2.03 Å R-free 0.219
7T3V Metal dependent activation of Plasmodium falciparum M17 aminopeptidase, spacegroup P22121 after crystals soaked with Zn2+ Deposited 2021-12-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 85–605（521 aa）
Chain B 85–605（521 aa）
Chain C 85–605（521 aa）
Chain D 85–605（521 aa）
Chain E 85–605（521 aa）
Chain F 85–605（521 aa）
Not recorded CO3 CARBONATE ION × 6 ZN ZINC ION × 12 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；50 mM HEPES pH 8.0, 150 mM NaCl
Resolution 2.30 Å R-free 0.264
8EZ4 Plasmodium falciparum M17 in complex with inhibitor 9aa Deposited 2022-10-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 85–605（521 aa）
Chain B 85–605（521 aa）
Chain C 85–605（521 aa）
Chain D 85–605（521 aa）
Chain E 85–605（521 aa）
Chain F 85–605（521 aa）
Not recorded X10 N-[(1R)-2-(hydroxyamino)-2-oxo-1-(3',4',5'-trifluoro[1,1'-biphenyl]-4-yl)ethyl]-N~2~-phenylglycinamide × 6 SO4 SULFATE ION × 7 1PE PENTAETHYLENE GLYCOL × 16 CO3 CARBONATE ION × 6 ZN ZINC ION × 12 NA SODIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；30-40% PEG400, 0.1 M Tris pH 7.5-8.5, 0.2 M Li2SO4
Resolution 1.89 Å R-free 0.216
8EZ4 Plasmodium falciparum M17 in complex with inhibitor 9aa Deposited 2022-10-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 85–605（521 aa）
Chain H 85–605（521 aa）
Chain I 85–605（521 aa）
Chain J 85–605（521 aa）
Chain K 85–605（521 aa）
Chain L 85–605（521 aa）
Not recorded X10 N-[(1R)-2-(hydroxyamino)-2-oxo-1-(3',4',5'-trifluoro[1,1'-biphenyl]-4-yl)ethyl]-N~2~-phenylglycinamide × 6 SO4 SULFATE ION × 6 1PE PENTAETHYLENE GLYCOL × 14 CO3 CARBONATE ION × 6 ZN ZINC ION × 12 NA SODIUM ION × 5 2PE NONAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；30-40% PEG400, 0.1 M Tris pH 7.5-8.5, 0.2 M Li2SO4
Resolution 1.89 Å R-free 0.216
8SVM Plasmodium falciparum M17 aminopeptidase bound to MMV1557817 Deposited 2023-05-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 84–605（522 aa）
Chain B 84–605（522 aa）
Chain C 84–605（522 aa）
Chain D 84–605（522 aa）
Chain E 84–605（522 aa）
Chain F 84–605（522 aa）
Not recorded CO3 CARBONATE ION × 6 ZN ZINC ION × 12 WRC N-[(1R)-2-(hydroxyamino)-2-oxo-1-(3',4',5'-trifluoro[1,1'-biphenyl]-4-yl)ethyl]-3,3-dimethylbutanamide × 6 1PE PENTAETHYLENE GLYCOL × 15 SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% (v/v) PEG 400, 0.1 M Tris pH 8.5, 0.2 M Li2SO4
Resolution 2.30 Å R-free 0.252
8SVM Plasmodium falciparum M17 aminopeptidase bound to MMV1557817 Deposited 2023-05-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 84–605（522 aa）
Chain H 84–605（522 aa）
Chain I 84–605（522 aa）
Chain J 84–605（522 aa）
Chain K 84–605（522 aa）
Chain L 84–605（522 aa）
Not recorded CO3 CARBONATE ION × 6 ZN ZINC ION × 12 WRC N-[(1R)-2-(hydroxyamino)-2-oxo-1-(3',4',5'-trifluoro[1,1'-biphenyl]-4-yl)ethyl]-3,3-dimethylbutanamide × 6 1PE PENTAETHYLENE GLYCOL × 13 SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% (v/v) PEG 400, 0.1 M Tris pH 8.5, 0.2 M Li2SO4
Resolution 2.30 Å R-free 0.252
8SW9 Plasmodium falciparum M17 (A460S) mutant Deposited 2023-05-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 84–605（522 aa）
Chain B 84–605（522 aa）
Chain C 84–605（522 aa）
Chain D 84–605（522 aa）
Chain E 84–605（522 aa）
Chain F 84–605（522 aa）
Not recorded ZN ZINC ION × 12 CO3 CARBONATE ION × 6 SO4 SULFATE ION × 8 1PE PENTAETHYLENE GLYCOL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% (v/v) PEG 400, 0.1 M Tris pH 8.5, 0.2 M Li2SO4
Resolution 2.60 Å R-free 0.281
8SW9 Plasmodium falciparum M17 (A460S) mutant Deposited 2023-05-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 84–605（522 aa）
Chain H 84–605（522 aa）
Chain I 84–605（522 aa）
Chain J 84–605（522 aa）
Chain K 84–605（522 aa）
Chain L 84–605（522 aa）
Not recorded ZN ZINC ION × 12 CO3 CARBONATE ION × 6 SO4 SULFATE ION × 9 1PE PENTAETHYLENE GLYCOL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；40% (v/v) PEG 400, 0.1 M Tris pH 8.5, 0.2 M Li2SO4
Resolution 2.60 Å R-free 0.281
9YC0 Plasmodium falciparum M17 aminopeptidase (PfA-M17) bound to inhibitor 3ab (MIPS3413) Deposited 2025-09-17 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 85–605（521 aa）
Chain B 85–605（521 aa）
Chain C 85–605（521 aa）
Chain D 85–605（521 aa）
Chain E 85–605（521 aa）
Chain F 85–605（521 aa）
Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q ZN ZINC ION × 12 CO3 CARBONATE ION × 6 PEG DI(HYDROXYETHYL)ETHER × 20 SO4 SULFATE ION × 29 A1CT4 N-[(1R)-1-(1,3-benzothiazol-5-yl)-2-(hydroxyamino)-2-oxoethyl]-3,3-dimethylbutanamide × 6 1PE PENTAETHYLENE GLYCOL × 16 DMS DIMETHYL SULFOXIDE × 7 2PE NONAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；30-40% PEG400, 0.1 M Tris pH 7.5-8.5, 0.2 M Li2SO4
Resolution 2.37 Å R-free 0.271
9YC0 Plasmodium falciparum M17 aminopeptidase (PfA-M17) bound to inhibitor 3ab (MIPS3413) Deposited 2025-09-17 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 85–605（521 aa）
Chain H 85–605（521 aa）
Chain I 85–605（521 aa）
Chain J 85–605（521 aa）
Chain K 85–605（521 aa）
Chain L 85–605（521 aa）
Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q Mutation：N152Q, N515Q, N546Q ZN ZINC ION × 12 CO3 CARBONATE ION × 6 PEG DI(HYDROXYETHYL)ETHER × 16 SO4 SULFATE ION × 30 A1CT4 N-[(1R)-1-(1,3-benzothiazol-5-yl)-2-(hydroxyamino)-2-oxoethyl]-3,3-dimethylbutanamide × 5 1PE PENTAETHYLENE GLYCOL × 21 DMS DIMETHYL SULFOXIDE × 6 2PE NONAETHYLENE GLYCOL × 1 A1CT5 N-[(1S)-1-(1,3-benzothiazol-5-yl)-2-(hydroxyamino)-2-oxoethyl]-3,3-dimethylbutanamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；30-40% PEG400, 0.1 M Tris pH 7.5-8.5, 0.2 M Li2SO4
Resolution 2.37 Å R-free 0.271
9YC7 Plasmodium falciparum M17 aminopeptidase (PfA-M17) bound to inhibitor 3k (MIPS3415) Deposited 2025-09-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 85–605（521 aa）
Chain B 85–605（521 aa）
Chain C 85–605（521 aa）
Chain D 85–605（521 aa）
Chain E 85–605（521 aa）
Chain F 85–605（521 aa）
Not recorded ZN ZINC ION × 12 CO3 CARBONATE ION × 6 PEG DI(HYDROXYETHYL)ETHER × 23 DMS DIMETHYL SULFOXIDE × 10 SO4 SULFATE ION × 12 GOL GLYCEROL × 1 A1CTH N-[(1R)-2-(hydroxyamino)-2-oxo-1-(quinolin-7-yl)ethyl]-3,3-dimethylbutanamide × 1 1PE PENTAETHYLENE GLYCOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；30-40% PEG400, 0.1 M Tris pH 7.5-8.5, 0.2 M Li2SO4
Resolution 2.37 Å R-free 0.287
9YC7 Plasmodium falciparum M17 aminopeptidase (PfA-M17) bound to inhibitor 3k (MIPS3415) Deposited 2025-09-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain G 85–605（521 aa）
Chain H 85–605（521 aa）
Chain I 85–605（521 aa）
Chain J 85–605（521 aa）
Chain K 85–605（521 aa）
Chain L 85–605（521 aa）
Not recorded ZN ZINC ION × 12 CO3 CARBONATE ION × 6 PEG DI(HYDROXYETHYL)ETHER × 20 DMS DIMETHYL SULFOXIDE × 9 SO4 SULFATE ION × 11 GOL GLYCEROL × 1 1PE PENTAETHYLENE GLYCOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；30-40% PEG400, 0.1 M Tris pH 7.5-8.5, 0.2 M Li2SO4
Resolution 2.37 Å R-free 0.287

16 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8IL11_PLAF7
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–522； UniProt 84–605 Author chain B； PDBConstruct 1–522； UniProt 84–605 Author chain C； PDBConstruct 1–522； UniProt 84–605 Author chain D； PDBConstruct 1–522； UniProt 84–605 Author chain E； PDBConstruct 1–522； UniProt 84–605 Author chain F； PDBConstruct 1–522； UniProt 84–605 Author chain G； PDBConstruct 1–522； UniProt 84–605 Author chain H； PDBConstruct 1–522； UniProt 84–605 Author chain I； PDBConstruct 1–522； UniProt 84–605 Author chain J； PDBConstruct 1–522； UniProt 84–605 Author chain K； PDBConstruct 1–522； UniProt 84–605 Author chain L； PDBConstruct 1–522； UniProt 84–605

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 3kqz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3kqz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3kqz
Deposition date deposition_date2009-11-17
Structure title titleStructure of a protease 2
Keywords keywordsprotease, Aminopeptidase, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier69.38 Å
Radius of gyration Rg (electron density) rg_electron69.61 Å
Forward intensity I(0) i05993060000.00
Molecular weight molecular_weight676870.0 kDa
Excluded volume excluded_volume853820 ų
Envelope volume envelope_volume1124000 ų
Hydration-shell volume shell_volume133100 ų
Envelope diameter envelope_diameter239.3 Å
Shell Rg shell_rg69.00 Å
Envelope Rg envelope_rg68.48 Å
Shape Rg shape_rg69.64 Å
Total Rg total_rg69.48 Å
Total atoms total_atoms47539
Residues n_residues6145
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax215.2 Å
Rg (real space) rg_real69.57 Å
Rg uncertainty (real space) rg_real_error1.38 Å
I(0) (real space) i0_real5.9900e+09
I(0) uncertainty (real space) i0_real_error1.0750e+08
Rg (reciprocal space) rg_reciprocal68.36 Å
I(0) (reciprocal space) i0_reciprocal5978000000.0000
Solution quality estimate total_estimate0.5730
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.1 Å
Skewness Skewness skewness0.412
Kurtosis Kurtosis kurtosis-0.653
Angular range angular_range— – 0.1150 Å−1
Current regularization parameter α current_alpha0.0102
Highest regularization parameter α highest_alpha1750000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 1.000; Sysdev: 0.002; Positv: 1.000; Valcen: 0.988; Smooth: 0.014
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

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7. Fold Classification (SCOP + CATH) 24 domains

CATH v4.4 (24 domains)

Domain ID domain_id3kqzA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzD02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzE01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzE02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzF01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzF02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzG01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzG02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzH01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzH02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzI01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzI02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzJ01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzJ02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzK01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzK02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqzL01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology220 — Leucine Aminopeptidase, subunit E; domain 1
Homologous superfamily homologous superfamily10 — Leucine Aminopeptidase, subunit E, domain 1
Domain ID domain_id3kqzL02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
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8. Citations (1)

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9. Files and Curves (10)