9cca

Cryo-EM structure of a designed pyridoxal phosphate (PLP) synthase fused to a designed circumsporozoite protein antigen from Plasmodium falciparum (CSP-P1-CSP and CSP-P2-CSP)

Method: ELECTRON MICROSCOPY D_max: 167.8 Å Quality: REASONABLE

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1. Protein Identity and Related Structures Protein Identity & Related Structures

;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit Pdx1 ;

Plasmodium falciparum

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 2–301 Chain B； UniProt 2–301 Chain C； UniProt 2–301 Chain D； UniProt 2–301 Chain E； UniProt 2–301 Chain F； UniProt 2–301 Chain M； UniProt 2–301 Chain N； UniProt 2–301 Chain O； UniProt 2–301 Chain P； UniProt 2–301 Chain Q； UniProt 2–301 Chain R； UniProt 2–301	Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C)	;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit PDX2 ; × 12 （Q7K740,Q8IIK4）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.95 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	PDX1_PLAF7
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 117–416； UniProt 2–301 Author chain B； PDBConstruct 117–416； UniProt 2–301 Author chain C； PDBConstruct 117–416； UniProt 2–301 Author chain D； PDBConstruct 117–416； UniProt 2–301 Author chain E； PDBConstruct 117–416； UniProt 2–301 Author chain F； PDBConstruct 117–416； UniProt 2–301 Author chain M； PDBConstruct 117–416； UniProt 2–301 Author chain N； PDBConstruct 117–416； UniProt 2–301 Author chain O； PDBConstruct 117–416； UniProt 2–301 Author chain P； PDBConstruct 117–416； UniProt 2–301 Author chain Q； PDBConstruct 117–416； UniProt 2–301 Author chain R； PDBConstruct 117–416； UniProt 2–301

;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit Pdx1 ;

Plasmodium falciparum

UniProt Q7K740

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 101–114 Chain A； UniProt 101–114 Chain A； UniProt 131–150 Chain A； UniProt 131–150 Chain A； UniProt 310–383 Chain A； UniProt 310–383 Chain B； UniProt 101–114 Chain B； UniProt 101–114 Chain B； UniProt 131–150 Chain B； UniProt 131–150 Chain B； UniProt 310–383 Chain B； UniProt 310–383 Chain C； UniProt 101–114 Chain C； UniProt 101–114 Chain C； UniProt 131–150 Chain C； UniProt 131–150 Chain C； UniProt 310–383 Chain C； UniProt 310–383 Chain D； UniProt 101–114 Chain D； UniProt 101–114 Chain D； UniProt 131–150 Chain D； UniProt 131–150 Chain D； UniProt 310–383 Chain D； UniProt 310–383 Chain E； UniProt 101–114 Chain E； UniProt 101–114 Chain E； UniProt 131–150 Chain E； UniProt 131–150 Chain E； UniProt 310–383 Chain E； UniProt 310–383 Chain F； UniProt 101–114 Chain F； UniProt 101–114 Chain F； UniProt 131–150 Chain F； UniProt 131–150 Chain F； UniProt 310–383 Chain F； UniProt 310–383 Chain G； UniProt 101–114 Chain G； UniProt 101–114 Chain G； UniProt 131–150 Chain G； UniProt 131–150 Chain G； UniProt 310–383 Chain G； UniProt 310–383 Chain H； UniProt 101–114 Chain H； UniProt 101–114 Chain H； UniProt 131–150 Chain H； UniProt 131–150 Chain H； UniProt 310–383 Chain H； UniProt 310–383 Chain I； UniProt 101–114 Chain I； UniProt 101–114 Chain I； UniProt 131–150 Chain I； UniProt 131–150 Chain I； UniProt 310–383 Chain I； UniProt 310–383 Chain J； UniProt 101–114 Chain J； UniProt 101–114 Chain J； UniProt 131–150 Chain J； UniProt 131–150 Chain J； UniProt 310–383 Chain J； UniProt 310–383 Chain K； UniProt 101–114 Chain K； UniProt 101–114 Chain K； UniProt 131–150 Chain K； UniProt 131–150 Chain K； UniProt 310–383 Chain K； UniProt 310–383 Chain L； UniProt 101–114 Chain L； UniProt 101–114 Chain L； UniProt 131–150 Chain L； UniProt 131–150 Chain L； UniProt 310–383 Chain L； UniProt 310–383 Chain M； UniProt 101–114 Chain M； UniProt 101–114 Chain M； UniProt 131–150 Chain M； UniProt 131–150 Chain M； UniProt 310–383 Chain M； UniProt 310–383 Chain N； UniProt 101–114 Chain N； UniProt 101–114 Chain N； UniProt 131–150 Chain N； UniProt 131–150 Chain N； UniProt 310–383 Chain N； UniProt 310–383 Chain O； UniProt 101–114 Chain O； UniProt 101–114 Chain O； UniProt 131–150 Chain O； UniProt 131–150 Chain O； UniProt 310–383 Chain O； UniProt 310–383 Chain P； UniProt 101–114 Chain P； UniProt 101–114 Chain P； UniProt 131–150 Chain P； UniProt 131–150 Chain P； UniProt 310–383 Chain P； UniProt 310–383 Chain Q； UniProt 101–114 Chain Q； UniProt 101–114 Chain Q； UniProt 131–150 Chain Q； UniProt 131–150 Chain Q； UniProt 310–383 Chain Q； UniProt 310–383 Chain R； UniProt 101–114 Chain R； UniProt 101–114 Chain R； UniProt 131–150 Chain R； UniProt 131–150 Chain R； UniProt 310–383 Chain R； UniProt 310–383 Chain S； UniProt 101–114 Chain S； UniProt 101–114 Chain S； UniProt 131–150 Chain S； UniProt 131–150 Chain S； UniProt 310–383 Chain S； UniProt 310–383 Chain T； UniProt 101–114 Chain T； UniProt 101–114 Chain T； UniProt 131–150 Chain T； UniProt 131–150 Chain T； UniProt 310–383 Chain T； UniProt 310–383 Chain U； UniProt 101–114 Chain U； UniProt 101–114 Chain U； UniProt 131–150 Chain U； UniProt 131–150 Chain U； UniProt 310–383 Chain U； UniProt 310–383 Chain V； UniProt 101–114 Chain V； UniProt 101–114 Chain V； UniProt 131–150 Chain V； UniProt 131–150 Chain V； UniProt 310–383 Chain V； UniProt 310–383 Chain W； UniProt 101–114 Chain W； UniProt 101–114 Chain W； UniProt 131–150 Chain W； UniProt 131–150 Chain W； UniProt 310–383 Chain W； UniProt 310–383 Chain X； UniProt 101–114 Chain X； UniProt 101–114 Chain X； UniProt 131–150 Chain X； UniProt 131–150 Chain X； UniProt 310–383 Chain X； UniProt 310–383	Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N)	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.95 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9CCA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3VDJ Crystal structure of circumsporozoite protein aTSR domain, R32 native form Deposited 2012-01-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；295 K；0.1 M citrate, pH 4.0, 1 M lithium chloride, 20% PEG6000, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.70 Å R-free 0.200
3VDJ Crystal structure of circumsporozoite protein aTSR domain, R32 native form Deposited 2012-01-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；295 K；0.1 M citrate, pH 4.0, 1 M lithium chloride, 20% PEG6000, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.70 Å R-free 0.200
3VDK Crystal structure of circumsporozoite protein aTSR domain, R32 platinum-bound form Deposited 2012-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374)	Not recorded	PT PLATINUM (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；295 K；0.1 M citrate, pH 4.0, 1 M lithium chloride, 20% PEG6000, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.85 Å R-free 0.217
3VDK Crystal structure of circumsporozoite protein aTSR domain, R32 platinum-bound form Deposited 2012-01-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374)	Not recorded	PT PLATINUM (II) ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；295 K；0.1 M citrate, pH 4.0, 1 M lithium chloride, 20% PEG6000, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.85 Å R-free 0.217
3VDL Crystal structure of circumsporozoite protein aTSR domain, P43212 form Deposited 2012-01-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；295 K；1.4 M sodium citrate, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.04 Å R-free 0.240
3VDL Crystal structure of circumsporozoite protein aTSR domain, P43212 form Deposited 2012-01-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；295 K；1.4 M sodium citrate, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.04 Å R-free 0.240
3VDL Crystal structure of circumsporozoite protein aTSR domain, P43212 form Deposited 2012-01-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；295 K；1.4 M sodium citrate, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.04 Å R-free 0.240
3VDL Crystal structure of circumsporozoite protein aTSR domain, P43212 form Deposited 2012-01-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374) Chain B 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374) Chain C 310–374（65 aa） Fragment：alpha-TSR domain (UNP residues 310-374)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；295 K；1.4 M sodium citrate, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.04 Å R-free 0.240
7RXI Fab234 in complex with the C-terminal alpha-TSR domain of P. falciparum Deposited 2021-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 310–375（66 aa） Fragment：C-terminal alpha-TSR domain (UNP residues 310-375)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；20% PEG8000, 0.1 M HEPES, pH 7.5	Resolution 2.15 Å R-free 0.265
7RXJ Fab236 in complex with the C-terminal alpha-TSR domain of P. falciparum Deposited 2021-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 310–375（66 aa） Fragment：C-terminal alpha-TSR domain (UNP residues 310-375)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；293.15 K；30% PEG2000 MME, 0.2 M ammonium sulfate, 0.1 M acetate, pH 4.6	Resolution 2.35 Å R-free 0.249
7RXJ Fab236 in complex with the C-terminal alpha-TSR domain of P. falciparum Deposited 2021-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 310–375（66 aa） Fragment：C-terminal alpha-TSR domain (UNP residues 310-375)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；293.15 K；30% PEG2000 MME, 0.2 M ammonium sulfate, 0.1 M acetate, pH 4.6	Resolution 2.35 Å R-free 0.249
7RXL Fab1488 in complex with the C-terminal alpha-TSR domain of P. falciparum Deposited 2021-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 310–375（66 aa） Fragment：C-terminal alpha-TSR domain (UNP residues 310-375)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.9；293.15 K；20% PEG3350, 0.2 M potassium chloride, pH 6.9	Resolution 1.82 Å R-free 0.255
7RXL Fab1488 in complex with the C-terminal alpha-TSR domain of P. falciparum Deposited 2021-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 310–375（66 aa） Fragment：C-terminal alpha-TSR domain (UNP residues 310-375)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.9；293.15 K；20% PEG3350, 0.2 M potassium chloride, pH 6.9	Resolution 1.82 Å R-free 0.255
7RXP Fab1512 in complex with the C-terminal alpha-TSR domain of P. falciparum Deposited 2021-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 309–375（67 aa） Fragment：C-terminal alpha-TSR domain (UNP residues 309-375)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；20% PEG3000, 0.2 M sodium chloride, 0.1 M HEPES. pH 7.5	Resolution 1.76 Å R-free 0.205
7S0X Fab352 in complex with the C-terminal alphaTSR domain of P. falciparum Deposited 2021-08-31	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 310–375（66 aa） Fragment：C-terminal alpha-TSR domain (UNP residues 310-375)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293.15 K；20% isopropanol, 20% PEG4000, 0.1 M sodium citrate, pH 5.6	Resolution 2.80 Å R-free 0.276
7S0X Fab352 in complex with the C-terminal alphaTSR domain of P. falciparum Deposited 2021-08-31	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 310–375（66 aa） Fragment：C-terminal alpha-TSR domain (UNP residues 310-375)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293.15 K；20% isopropanol, 20% PEG4000, 0.1 M sodium citrate, pH 5.6	Resolution 2.80 Å R-free 0.276
7V05 Complex of Plasmodium falciparum circumsporozoite protein with 850 Fab Deposited 2022-05-09	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric	Chain X 20–384（365 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.40 Å
8EK1 Cryo-EM structure of a potent anti-malarial antibody L9 in complex with Plasmodium falciparum circumsporozoite protein (PfCSP)(dominant class) Deposited 2022-09-19	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain P 21–375（355 aa）	Mutation：C-79S, K-38S, K-37S, R-34A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
8EKA Cryo-EM structure of a potent anti-malarial antibody L9 in complex with Plasmodium falciparum circumsporozoite protein (PfCSP)(class 2) Deposited 2022-09-20	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain P 21–375（355 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8FG0 Crystal structure of the 3764 Fab in complex with the C-terminal PfCSP linker, PfCSP281-294. Deposited 2022-12-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain P 281–294（14 aa） Fragment：residues 281-294	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；19% (v/v) isopropanol, 19% (w/v) PEG 4000, 5% (v/v) glycerol, 0.095 M sodium citrate, pH 5.6	Resolution 2.36 Å R-free 0.237
8FG0 Crystal structure of the 3764 Fab in complex with the C-terminal PfCSP linker, PfCSP281-294. Deposited 2022-12-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain Q 281–294（14 aa） Fragment：residues 281-294	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；19% (v/v) isopropanol, 19% (w/v) PEG 4000, 5% (v/v) glycerol, 0.095 M sodium citrate, pH 5.6	Resolution 2.36 Å R-free 0.237
9C79 Human monoclonal antibody MAD21-101 bound to the N-terminus of cleaved circumsporozoite protein Deposited 2024-06-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 96–113（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；277 K；2.0 M ammonium sulfate, 0.2 M sodium chloride, 0.1 M cacodylate	Resolution 1.46 Å R-free 0.200
9C7D Human monoclonal antibody MAD22-38 bound to the N-terminus of cleaved circumsporozoite protein Deposited 2024-06-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 96–113（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；20% PEG 3350, 0.2 M ammonium chloride	Resolution 1.99 Å R-free 0.232
9C7F Human monoclonal antibody MAD24-01 bound to the N-terminus of cleaved circumsporozoite protein Deposited 2024-06-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain J 96–113（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；20% PEG 3350 and 0.2 M potassium fluoride	Resolution 1.82 Å R-free 0.238
9C7F Human monoclonal antibody MAD24-01 bound to the N-terminus of cleaved circumsporozoite protein Deposited 2024-06-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 96–113（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；20% PEG 3350 and 0.2 M potassium fluoride	Resolution 1.82 Å R-free 0.238
9C7F Human monoclonal antibody MAD24-01 bound to the N-terminus of cleaved circumsporozoite protein Deposited 2024-06-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 96–113（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；20% PEG 3350 and 0.2 M potassium fluoride	Resolution 1.82 Å R-free 0.238
9C7F Human monoclonal antibody MAD24-01 bound to the N-terminus of cleaved circumsporozoite protein Deposited 2024-06-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain Q 96–113（18 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；277 K；20% PEG 3350 and 0.2 M potassium fluoride	Resolution 1.82 Å R-free 0.238
9DSR Crystal structure of Fab MS-1805 in complex with NPNA3 peptide from circumsporozoite protein Deposited 2024-09-28	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 131–142（12 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M Zinc acetate, 20% (w/v) polyethylene glycol	Resolution 2.25 Å R-free 0.239
9DSS Crystal structure of Fab 7088 in complex with NPNA3 peptide from circumsporozoite protein Deposited 2024-09-28	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 131–142（12 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.2 M sodium chloride and 20% (w/v) polyethylene glycol 3350	Resolution 2.00 Å R-free 0.263
9DST Crystal structure of Fab MS-1805 in complex with N-terminal junction peptide from circumsporozoite protein Deposited 2024-09-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 95–110（16 aa）	Not recorded	CIT CITRIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.1 M sodium citrate, 20% (v/v) 2-propanol and 20% (w/v) polyethylene glycol 4000	Resolution 1.74 Å R-free 0.228
9DSU Crystal structure of Fab 7088 in complex with N-terminal junction peptide from circumsporozoite protein Deposited 2024-09-28	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 95–110（16 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293.15 K；0.1 M Tris pH 8.0, 1M lithium chloride and 10% (w/v) polyethylene glycol 6000	Resolution 3.14 Å R-free 0.275
9NCY Fab1392 in complex with the C-terminal alpha-TSR domain of the P. falciparum circumsporozoite protein Deposited 2025-02-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 310–376（67 aa）	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 5 GOL GLYCEROL × 8 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG-600, 10% (v/v) glycerol, 0.5 M NH4-sulfate, 0.1 M Tris pH 7.0, final pH 5.6.	Resolution 1.63 Å R-free 0.194
9NKZ Crystal structure of Fab MAM01 in complex with NANP6 peptide from circumsporozoite protein Deposited 2025-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 129–152（24 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.04 M potassium dihydrogen phosphate, 20% (v/v) glycerol and 16% (w/v) polyethylene glycol 8000	Resolution 1.48 Å R-free 0.210
9NL0 Crystal structure of Fab MAM01 in complex with NPNA3 peptide from circumsporozoite protein Deposited 2025-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 131–142（12 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.1 M Bicine pH 9.0 and 65% (v/v) 2-methyl-2,4-pentanediol	Resolution 1.54 Å R-free 0.202
9NL1 Crystal structure of Fab MAM01 in complex with junctional region peptide from circumsporozoite protein Deposited 2025-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 101–114（14 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.085 M Tris pH 8.5, 0.17 M sodium acetate, 15% (v/v) glycerol and 25.5 % (w/v) polyethylene glycol 4000	Resolution 2.71 Å R-free 0.313
9NZF Crystal structure of Fab MAM01 in complex with minor repeat region peptide from circumsporozoite protein Deposited 2025-03-31	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 109–128（20 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；0.2 M potassium acetate, pH 7.8 and 20% (w/v) polyethylene glycol 3350	Resolution 1.84 Å R-free 0.230
9ZM7 Crystal structure of Fab 7160 in complex with junctional region from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain K 101–116（16 aa） Chain L 101–116（16 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；293 K；0.2 M sodium dihydrogen phosphate (pH 4.5) and 20% (w/v) polyethylene glycol (PEG) 3350	Resolution 2.30 Å R-free 0.275
9ZM7 Crystal structure of Fab 7160 in complex with junctional region from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 101–116（16 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；293 K；0.2 M sodium dihydrogen phosphate (pH 4.5) and 20% (w/v) polyethylene glycol (PEG) 3350	Resolution 2.30 Å R-free 0.275
9ZM7 Crystal structure of Fab 7160 in complex with junctional region from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 101–116（16 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；293 K；0.2 M sodium dihydrogen phosphate (pH 4.5) and 20% (w/v) polyethylene glycol (PEG) 3350	Resolution 2.30 Å R-free 0.275
9ZM7 Crystal structure of Fab 7160 in complex with junctional region from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain O 101–116（16 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；293 K；0.2 M sodium dihydrogen phosphate (pH 4.5) and 20% (w/v) polyethylene glycol (PEG) 3350	Resolution 2.30 Å R-free 0.275
9ZM7 Crystal structure of Fab 7160 in complex with junctional region from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain R 101–116（16 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；293 K；0.2 M sodium dihydrogen phosphate (pH 4.5) and 20% (w/v) polyethylene glycol (PEG) 3350	Resolution 2.30 Å R-free 0.275
9ZM7 Crystal structure of Fab 7160 in complex with junctional region from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain U 101–116（16 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；293 K；0.2 M sodium dihydrogen phosphate (pH 4.5) and 20% (w/v) polyethylene glycol (PEG) 3350	Resolution 2.30 Å R-free 0.275
9ZM7 Crystal structure of Fab 7160 in complex with junctional region from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain X 101–116（16 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；293 K；0.2 M sodium dihydrogen phosphate (pH 4.5) and 20% (w/v) polyethylene glycol (PEG) 3350	Resolution 2.30 Å R-free 0.275
9ZM8 Crystal structure of 7160 in complex with minor repeat region from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 109–128（20 aa） Chain D 109–128（20 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293 K；0.1 M HEPES (pH 7.0), 1 M lithium chloride, and 20% (w/v) PEG 6000.	Resolution 2.27 Å R-free 0.286
9ZM9 Crystal structure of Fab 7160 in complex with short major repeat region (NPNA3) from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain E 131–142（12 aa） Chain F 131–142（12 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；0.2 M sodium acetate (pH 7.0) and 20% (w/v) PEG 3350.	Resolution 1.88 Å R-free 0.245
9ZMA Crystal structure of Fab 7160 in complex with major repeat region (NANP6)from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 129–152（24 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M magnesium nitrate (pH 5.8) and 20% (w/v) PEG 3350.	Resolution 2.33 Å R-free 0.236
9ZMA Crystal structure of Fab 7160 in complex with major repeat region (NANP6)from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain J 129–152（24 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.2 M magnesium nitrate (pH 5.8) and 20% (w/v) PEG 3350.	Resolution 2.33 Å R-free 0.236
9ZMB Crystal structure of Fab 7118 in complex with minor repeat region from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 109–128（20 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.1 M HEPES (pH 7.5), 30% (v/v) 1,2-propanediol, and 20% (v/v) PEG 400	Resolution 2.09 Å R-free 0.243
9ZMC Crystal structure of Fab 7118 in complex with major repeat region (NANP6) from circumsporozoite protein Deposited 2025-12-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 129–152（24 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M sodium cacodylate (pH 6.5), 0.16 M calcium acetate, 14.4% (w/v) PEG 8000, and 20% (v/v) glycerol	Resolution 2.00 Å R-free 0.217

30 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CSP_PLAF7
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 4–17； UniProt 101–114 Author chain A； PDBConstruct 419–432； UniProt 101–114 Author chain A； PDBConstruct 18–37； UniProt 131–150 Author chain A； PDBConstruct 433–452； UniProt 131–150 Author chain A； PDBConstruct 38–111； UniProt 310–383 Author chain A； PDBConstruct 453–526； UniProt 310–383 Author chain B； PDBConstruct 4–17； UniProt 101–114 Author chain B； PDBConstruct 419–432； UniProt 101–114 Author chain B； PDBConstruct 18–37； UniProt 131–150 Author chain B； PDBConstruct 433–452； UniProt 131–150 Author chain B； PDBConstruct 38–111； UniProt 310–383 Author chain B； PDBConstruct 453–526； UniProt 310–383 Author chain C； PDBConstruct 4–17； UniProt 101–114 Author chain C； PDBConstruct 419–432； UniProt 101–114 Author chain C； PDBConstruct 18–37； UniProt 131–150 Author chain C； PDBConstruct 433–452； UniProt 131–150 Author chain C； PDBConstruct 38–111； UniProt 310–383 Author chain C； PDBConstruct 453–526； UniProt 310–383 Author chain D； PDBConstruct 4–17； UniProt 101–114 Author chain D； PDBConstruct 419–432； UniProt 101–114 Author chain D； PDBConstruct 18–37； UniProt 131–150 Author chain D； PDBConstruct 433–452； UniProt 131–150 Author chain D； PDBConstruct 38–111； UniProt 310–383 Author chain D； PDBConstruct 453–526； UniProt 310–383 Author chain E； PDBConstruct 4–17； UniProt 101–114 Author chain E； PDBConstruct 419–432； UniProt 101–114 Author chain E； PDBConstruct 18–37； UniProt 131–150 Author chain E； PDBConstruct 433–452； UniProt 131–150 Author chain E； PDBConstruct 38–111； UniProt 310–383 Author chain E； PDBConstruct 453–526； UniProt 310–383 Author chain F； PDBConstruct 4–17； UniProt 101–114 Author chain F； PDBConstruct 419–432； UniProt 101–114 Author chain F； PDBConstruct 18–37； UniProt 131–150 Author chain F； PDBConstruct 433–452； UniProt 131–150 Author chain F； PDBConstruct 38–111； UniProt 310–383 Author chain F； PDBConstruct 453–526； UniProt 310–383 Author chain M； PDBConstruct 4–17； UniProt 101–114 Author chain M； PDBConstruct 419–432； UniProt 101–114 Author chain M； PDBConstruct 18–37； UniProt 131–150 Author chain M； PDBConstruct 433–452； UniProt 131–150 Author chain M； PDBConstruct 38–111； UniProt 310–383 Author chain M； PDBConstruct 453–526； UniProt 310–383 Author chain N； PDBConstruct 4–17； UniProt 101–114 Author chain N； PDBConstruct 419–432； UniProt 101–114 Author chain N； PDBConstruct 18–37； UniProt 131–150 Author chain N； PDBConstruct 433–452； UniProt 131–150 Author chain N； PDBConstruct 38–111； UniProt 310–383 Author chain N； PDBConstruct 453–526； UniProt 310–383 Author chain O； PDBConstruct 4–17； UniProt 101–114 Author chain O； PDBConstruct 419–432； UniProt 101–114 Author chain O； PDBConstruct 18–37； UniProt 131–150 Author chain O； PDBConstruct 433–452； UniProt 131–150 Author chain O； PDBConstruct 38–111； UniProt 310–383 Author chain O； PDBConstruct 453–526； UniProt 310–383 Author chain P； PDBConstruct 4–17； UniProt 101–114 Author chain P； PDBConstruct 419–432； UniProt 101–114 Author chain P； PDBConstruct 18–37； UniProt 131–150 Author chain P； PDBConstruct 433–452； UniProt 131–150 Author chain P； PDBConstruct 38–111； UniProt 310–383 Author chain P； PDBConstruct 453–526； UniProt 310–383 Author chain Q； PDBConstruct 4–17； UniProt 101–114 Author chain Q； PDBConstruct 419–432； UniProt 101–114 Author chain Q； PDBConstruct 18–37； UniProt 131–150 Author chain Q； PDBConstruct 433–452； UniProt 131–150 Author chain Q； PDBConstruct 38–111； UniProt 310–383 Author chain Q； PDBConstruct 453–526； UniProt 310–383 Author chain R； PDBConstruct 4–17； UniProt 101–114 Author chain R； PDBConstruct 419–432； UniProt 101–114 Author chain R； PDBConstruct 18–37； UniProt 131–150 Author chain R； PDBConstruct 433–452； UniProt 131–150 Author chain R； PDBConstruct 38–111； UniProt 310–383 Author chain R； PDBConstruct 453–526； UniProt 310–383 Author chain G； PDBConstruct 4–17； UniProt 101–114 Author chain G； PDBConstruct 336–349； UniProt 101–114 Author chain G； PDBConstruct 18–37； UniProt 131–150 Author chain G； PDBConstruct 350–369； UniProt 131–150 Author chain G； PDBConstruct 38–111； UniProt 310–383 Author chain G； PDBConstruct 370–443； UniProt 310–383 Author chain H； PDBConstruct 4–17； UniProt 101–114 Author chain H； PDBConstruct 336–349； UniProt 101–114 Author chain H； PDBConstruct 18–37； UniProt 131–150 Author chain H； PDBConstruct 350–369； UniProt 131–150 Author chain H； PDBConstruct 38–111； UniProt 310–383 Author chain H； PDBConstruct 370–443； UniProt 310–383 Author chain I； PDBConstruct 4–17； UniProt 101–114 Author chain I； PDBConstruct 336–349； UniProt 101–114 Author chain I； PDBConstruct 18–37； UniProt 131–150 Author chain I； PDBConstruct 350–369； UniProt 131–150 Author chain I； PDBConstruct 38–111； UniProt 310–383 Author chain I； PDBConstruct 370–443； UniProt 310–383 Author chain J； PDBConstruct 4–17； UniProt 101–114 Author chain J； PDBConstruct 336–349； UniProt 101–114 Author chain J； PDBConstruct 18–37； UniProt 131–150 Author chain J； PDBConstruct 350–369； UniProt 131–150 Author chain J； PDBConstruct 38–111； UniProt 310–383 Author chain J； PDBConstruct 370–443； UniProt 310–383 Author chain K； PDBConstruct 4–17； UniProt 101–114 Author chain K； PDBConstruct 336–349； UniProt 101–114 Author chain K； PDBConstruct 18–37； UniProt 131–150 Author chain K； PDBConstruct 350–369； UniProt 131–150 Author chain K； PDBConstruct 38–111； UniProt 310–383 Author chain K； PDBConstruct 370–443； UniProt 310–383 Author chain L； PDBConstruct 4–17； UniProt 101–114 Author chain L； PDBConstruct 336–349； UniProt 101–114 Author chain L； PDBConstruct 18–37； UniProt 131–150 Author chain L； PDBConstruct 350–369； UniProt 131–150 Author chain L； PDBConstruct 38–111； UniProt 310–383 Author chain L； PDBConstruct 370–443； UniProt 310–383 Author chain S； PDBConstruct 4–17； UniProt 101–114 Author chain S； PDBConstruct 336–349； UniProt 101–114 Author chain S； PDBConstruct 18–37； UniProt 131–150 Author chain S； PDBConstruct 350–369； UniProt 131–150 Author chain S； PDBConstruct 38–111； UniProt 310–383 Author chain S； PDBConstruct 370–443； UniProt 310–383 Author chain T； PDBConstruct 4–17； UniProt 101–114 Author chain T； PDBConstruct 336–349； UniProt 101–114 Author chain T； PDBConstruct 18–37； UniProt 131–150 Author chain T； PDBConstruct 350–369； UniProt 131–150 Author chain T； PDBConstruct 38–111； UniProt 310–383 Author chain T； PDBConstruct 370–443； UniProt 310–383 Author chain U； PDBConstruct 4–17； UniProt 101–114 Author chain U； PDBConstruct 336–349； UniProt 101–114 Author chain U； PDBConstruct 18–37； UniProt 131–150 Author chain U； PDBConstruct 350–369； UniProt 131–150 Author chain U； PDBConstruct 38–111； UniProt 310–383 Author chain U； PDBConstruct 370–443； UniProt 310–383 Author chain V； PDBConstruct 4–17； UniProt 101–114 Author chain V； PDBConstruct 336–349； UniProt 101–114 Author chain V； PDBConstruct 18–37； UniProt 131–150 Author chain V； PDBConstruct 350–369； UniProt 131–150 Author chain V； PDBConstruct 38–111； UniProt 310–383 Author chain V； PDBConstruct 370–443； UniProt 310–383 Author chain W； PDBConstruct 4–17； UniProt 101–114 Author chain W； PDBConstruct 336–349； UniProt 101–114 Author chain W； PDBConstruct 18–37； UniProt 131–150 Author chain W； PDBConstruct 350–369； UniProt 131–150 Author chain W； PDBConstruct 38–111； UniProt 310–383 Author chain W； PDBConstruct 370–443； UniProt 310–383 Author chain X； PDBConstruct 4–17； UniProt 101–114 Author chain X； PDBConstruct 336–349； UniProt 101–114 Author chain X； PDBConstruct 18–37； UniProt 131–150 Author chain X； PDBConstruct 350–369； UniProt 131–150 Author chain X； PDBConstruct 38–111； UniProt 310–383 Author chain X； PDBConstruct 370–443； UniProt 310–383

;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit PDX2 ;

Plasmodium falciparum

UniProt Q8IIK4

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain G； UniProt 3–219 Chain H； UniProt 3–219 Chain I； UniProt 3–219 Chain J； UniProt 3–219 Chain K； UniProt 3–219 Chain L； UniProt 3–219 Chain S； UniProt 3–219 Chain T； UniProt 3–219 Chain U； UniProt 3–219 Chain V； UniProt 3–219 Chain W； UniProt 3–219 Chain X； UniProt 3–219	Mutation：N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N)	;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit Pdx1 ; × 12 （Q7K740,C6KT50）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.95 Å

Other States of the Same Protein in the Database

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	PDX2_PLAF7
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 117–333； UniProt 3–219 Author chain H； PDBConstruct 117–333； UniProt 3–219 Author chain I； PDBConstruct 117–333； UniProt 3–219 Author chain J； PDBConstruct 117–333； UniProt 3–219 Author chain K； PDBConstruct 117–333； UniProt 3–219 Author chain L； PDBConstruct 117–333； UniProt 3–219 Author chain S； PDBConstruct 117–333； UniProt 3–219 Author chain T； PDBConstruct 117–333； UniProt 3–219 Author chain U； PDBConstruct 117–333； UniProt 3–219 Author chain V； PDBConstruct 117–333； UniProt 3–219 Author chain W； PDBConstruct 117–333； UniProt 3–219 Author chain X； PDBConstruct 117–333； UniProt 3–219

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9cca
Deposition date deposition_date	2024-06-21
Structure title title	Cryo-EM structure of a designed pyridoxal phosphate (PLP) synthase fused to a designed circumsporozoite protein antigen from Plasmodium falciparum (CSP-P1-CSP and CSP-P2-CSP)
Keywords keywords	synthase, complex, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	60.45 Å
Radius of gyration Rg (electron density) rg_electron	60.19 Å
Forward intensity I(0) i0	4468900000.00
Molecular weight molecular_weight	580830.0 kDa
Excluded volume excluded_volume	734380 Å³
Envelope volume envelope_volume	1103500 Å³
Hydration-shell volume shell_volume	146940 Å³
Envelope diameter envelope_diameter	176.5 Å
Shell Rg shell_rg	69.05 Å
Envelope Rg envelope_rg	57.26 Å
Shape Rg shape_rg	60.25 Å
Total Rg total_rg	60.18 Å
Total atoms total_atoms	82341
Residues n_residues	5287
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	167.8 Å
Rg (real space) rg_real	59.94 Å
Rg uncertainty (real space) rg_real_error	0.95 Å
I(0) (real space) i0_real	4.4690e+09
I(0) uncertainty (real space) i0_real_error	7.9550e+07
Rg (reciprocal space) rg_reciprocal	60.86 Å
I(0) (reciprocal space) i0_reciprocal	4475000000.0000
Solution quality estimate total_estimate	0.6161
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	77.4 Å
Skewness Skewness skewness	-0.038
Kurtosis Kurtosis kurtosis	-0.510
Angular range angular_range	— – 0.1300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	122000000.0000
Real-space data points n_real_points	27
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.969; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 1.000; Smooth: 0.023

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit Pdx1 ;
Molecular weight formula_weight	58417.1 kDa
EC 编号 ec_number	4.3.3.6
Mutation mutation	K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C)
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,M,N,O,P,Q,R
Atom count atom_count	82341

MTGNPDPNANPNVDPNANPNANPNANPNANPNANPNAEPSDKHIKEYLNKIQNSLSTEWSPCSVTCGNGIQVRIKPGSANKPKDELDYANDIEKKICKMEKCSSVFNVVNSGGSGTENHKDDAVLLKHGWCEMLKGGVIMDVKSVEQAKIAEEAGAIGVMVLENIPSELRNKEGVARSVDPSKVEEIKKCVSINVLARVRIGHFVEAQILEELKIDMIDESEVLTIADEMHHIDKHKFKTPFVCGCTNLGEALRRISEGASMIRTKGEAGTGNIIEAIKHIRTVNNEICYLCCLSDSEVYHFAKKINAPIDLVLLTKKLKRLPVVNFAAGGVATPADAAMCMQLGMDGVFVGSGIFESENPRKMAASIVSAVSNFNNPKILLDVSMNLGKAMCGSTRVSDKWKNKNEEHTKFLTPQTGNPDPNANPNVDPNANPNANPNANPNANPNANPNAEPSDKHIKEYLNKIQNSLSTEWSPCSVTCGNGIQVRIKPGSANKPKDELDYANDIEKKICKMEKCSSVFNVVNSGGSLEHHHHHH

来源 Source

来源生物 organism	Plasmodium falciparum
通用名 common_name	malaria parasite P. falciparum
NCBI Class编号 ncbi_taxonomy_id	5833
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit PDX2 ;
Molecular weight formula_weight	49843.6 kDa
EC 编号 ec_number	4.3.3.6,3.5.1.2
Mutation mutation	N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N)
Source method src_method	man
Copy count entity_count	12

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,H,I,J,K,L,S,T,U,V,W,X

MTGNPDPNANPNVDPNANPNANPNANPNANPNANPNAEPSDKHIKEYLNKIQNSLSTEWSPCSVTCGNGIQVRIKPGSANKPKDELDYANDIEKKICKMEKCSSVFNVVNSGGSGTEITIGVLSLQGDFEPHINHFIKLQIPSLNIIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYEQDTLYNALVHFIHVLKKPIWGTCAGCILLSKNVENIKLYSNFGNKFSFGGLDITICRNFYGSQQDSFICSLNIISDSSAFKKDLTAACIRAPYIREILSDEVKVLATFSHESYGPNIIAAVEQNNCLGTVFNPELLPHTAFQQYFYEKVKNYKYSTGNPDPNANPNVDPNANPNANPNANPNANPNANPNAEPSDKHIKEYLNKIQNSLSTEWSPCSVTCGNGIQVRIKPGSANKPKDELDYANDIEKKICKMEKCSSVFNVVNSGGSLEHHHHHH

来源 Source

来源生物 organism	Plasmodium falciparum
通用名 common_name	malaria parasite P. falciparum
NCBI Class编号 ncbi_taxonomy_id	5833
宿主生物 host_organism	Escherichia coli

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	triclinic

Resolution resolution	2.95 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	251050

fit	/app/data/saxs_computation/cc/9cca/9cca.fit
pddf	/app/data/pr_computation/cc/9cca/9cca.pr.out
profile	/app/data/saxs_computation/cc/9cca/9cca.dat

Cryo-EM structure of a designed pyridoxal phosphate (PLP) synthase fused to a designed circumsporozoite protein antigen from Plasmodium falciparum (CSP-P1-CSP and CSP-P2-CSP)

1. Protein Identity and Related Structures Protein Identity & Related Structures

;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit Pdx1 ;

State in the Current Structure

Other States of the Same Protein in the Database

;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit Pdx1 ;

State in the Current Structure

Other States of the Same Protein in the Database

;Circumsporozoite protein,Pyridoxal 5'-phosphate synthase subunit PDX2 ;

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)