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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：C6KT50 New Search
1PDB entries
1Biological assembly
12chain/assembly records
Main Difference Dimensions in This Set
No difference found in parsed fields

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 A 2–301（300 aa）
Chain B 2–301（300 aa）
Chain C 2–301（300 aa）
Chain D 2–301（300 aa）
Chain E 2–301（300 aa）
Chain F 2–301（300 aa）
Chain M 2–301（300 aa）
Chain N 2–301（300 aa）
Chain O 2–301（300 aa）
Chain P 2–301（300 aa）
Chain Q 2–301（300 aa）
Chain R 2–301（300 aa）
Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) Mutation：K198R,K289C,S293C in Pdx1 (Uniprot numbering: K83R,K174C,S178C) No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.95 Å

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.