MolNFT v1 · #35136 · protein
Tpr domain of nrfg mediates the complex formation between heme lyase and formate-dependent nitrite reductase in escherichia COLI O157:H7
2E2E: “Tpr domain of nrfg mediates the complex formation between heme lyase and formate-dependent nitrite reductase…”. X-ray diffraction. MolNFT v1 #35136 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2E2E
- Type
- protein
- Length
- 342 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8X5S3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 171 | — | Q8X5S3 |
Compared structures
- 2E2E · TPR domain of NrfG mediates the complex formation between heme lyase and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8X5S3 · AlphaFold monomer V2.0 prediction for formate-dependent nitrite reductase complex subunit… · a predicted model of the same protein · chain A against A, TM-score 0.88
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q8X5S3
- Elsewhere: RCSB PDB 2E2E · PDBe 2E2E · UniProt Q8X5S3
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