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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：P0A603 New Search
6PDB entries
6Biological assembly
6chain/assembly records
Main Difference Dimensions in This Set
Different ligand/ion Different structure-quality metrics

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
9E7V Off-pathway Mycobacterium tuberculosis transcription initiation promoter complex (RNA Polymerase with Sigma-A, CarD, and RbpA) Deposited 2024-11-04 Assembly 1 Insufficient information Heteromer；Protein × 8 PDB declaration: decameric（10） Consistent with all polymers
Chain F 1–528（528 aa）
Not recorded POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9E7Y De Novo Mycobacterium tuberculosis transcription initiation promoter complex with 7-mer RNA and disordered Beta' Lid element (RNA Polymerase with Sigma-A, CarD, and RbpA) Deposited 2024-11-04 Assembly 1 Insufficient information Heteromer；Protein × 8 PDB declaration: undecameric（11） Consistent with all polymers
Chain F 1–528（528 aa）
Not recorded POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
9E84 De Novo Mycobacterium tuberculosis transcription initiation promoter complex with 6-mer RNA and disordered Sigma-A region 4 domain (RNA Polymerase with Sigma-A, CarD, and RbpA) Deposited 2024-11-05 Assembly 1 Insufficient information Heteromer；Protein × 8 PDB declaration: 11-meric（11） Consistent with all polymers
Chain F 1–528（528 aa）
Not recorded POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9E85 De Novo Mycobacterium tuberculosis transcription initiation promoter complex with 6-mer RNA and closed Beta' clamp (RNA Polymerase with Sigma-A, CarD, and RbpA) Deposited 2024-11-05 Assembly 1 Insufficient information Heteromer；Protein × 8 PDB declaration: 11-meric（11） Consistent with all polymers
Chain F 1–528（528 aa）
Not recorded POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
9E86 De Novo Mycobacterium tuberculosis transcription initiation promoter complex with 5-mer RNA and open Beta' clamp (RNA Polymerase with Sigma-A, CarD, and RbpA) Deposited 2024-11-05 Assembly 1 Insufficient information Heteromer；Protein × 8 PDB declaration: 11-meric（11） Consistent with all polymers
Chain F 1–528（528 aa）
Not recorded POP PYROPHOSPHATE 2- × 1 ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
9E87 De Novo Mycobacterium tuberculosis transcription initiation pre-RPO promoter complex with open Beta' clamp (RNA Polymerase with Sigma-A, CarD, and RbpA) Deposited 2024-11-05 Assembly 1 Insufficient information Heteromer；Protein × 8 PDB declaration: decameric（10） Consistent with all polymers
Chain F 1–528（528 aa）
Not recorded ZN ZINC ION × 2 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 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.