Current Protein Identity:Q8IIK4
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 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) Deposited 2024-06-21 | Assembly 1 Insufficient information Heteromer;Protein × 24 PDB declaration: 24-meric(24) Consistent with protein count |
Chain G
3–219(217 aa)
Chain H
3–219(217 aa)
Chain I
3–219(217 aa)
Chain J
3–219(217 aa)
Chain K
3–219(217 aa)
Chain L
3–219(217 aa)
Chain S
3–219(217 aa)
Chain T
3–219(217 aa)
Chain U
3–219(217 aa)
Chain V
3–219(217 aa)
Chain W
3–219(217 aa)
Chain X
3–219(217 aa)
|
Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) Mutation:N179Q,N242Q,H310N in Pdx2 (Uniprot numbering: N65Q,N128Q,H196N) | No recorded non-water small molecule | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.95 Å |