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3kqx

Structure of a protease 1

Method: X-RAY DIFFRACTION Dmax: 209.9 Å Quality: GOOD
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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 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
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 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

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 3KQX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3KQZ Structure of a protease 2 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 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
3KQZ Structure of a protease 2 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 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
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 3kqx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3kqx
Deposition date deposition_date2009-11-17
Structure title titleStructure of a protease 1
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_guinier70.54 Å
Radius of gyration Rg (electron density) rg_electron70.75 Å
Forward intensity I(0) i05908060000.00
Molecular weight molecular_weight675170.0 kDa
Excluded volume excluded_volume853040 ų
Envelope volume envelope_volume1163800 ų
Hydration-shell volume shell_volume135720 ų
Envelope diameter envelope_diameter243.9 Å
Shell Rg shell_rg69.84 Å
Envelope Rg envelope_rg69.52 Å
Shape Rg shape_rg70.78 Å
Total Rg total_rg70.65 Å
Total atoms total_atoms47480
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 dmax209.9 Å
Rg (real space) rg_real70.49 Å
Rg uncertainty (real space) rg_real_error1.03 Å
I(0) (real space) i0_real5.8950e+09
I(0) uncertainty (real space) i0_real_error1.0660e+08
Rg (reciprocal space) rg_reciprocal69.45 Å
I(0) (reciprocal space) i0_reciprocal5892000000.0000
Solution quality estimate total_estimate0.8110
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.3 Å
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.680
Angular range angular_range— – 0.1100 Å−1
Current regularization parameter α current_alpha0.0154
Highest regularization parameter α highest_alpha1884000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.002
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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_id3kqxA01
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_id3kqxA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxB01
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_id3kqxB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxC01
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_id3kqxC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxD01
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_id3kqxD02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxE01
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_id3kqxE02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxF01
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_id3kqxF02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxG01
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_id3kqxG02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxH01
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_id3kqxH02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxI01
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_id3kqxI02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxJ01
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_id3kqxJ02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxK01
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_id3kqxK02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology630 — Aminopeptidase
Homologous superfamily homologous superfamily10 — Zn peptidases
Domain ID domain_id3kqxL01
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_id3kqxL02
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)