MolNFT v1 · #145120 · protein
The AER2 receptor from vibrio cholerae is a dual pas-heme oxygen sensor
6CEQ: “The AER2 receptor from vibrio cholerae is a dual pas-heme oxygen sensor”. X-ray diffraction, 1 ligand (HEM). MolNFT v1 #145120 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6CEQ
- Type
- protein
- Length
- 333 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2D2BEZ7
- Ligands
- HEM
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 111 | — | A0A2D2BEZ7 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6CEQ · The Aer2 Receptor from Vibrio cholerae is a Dual PAS-Heme Oxygen Sensor · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A2D2BEZ7
- Elsewhere: RCSB PDB 6CEQ · PDBe 6CEQ · UniProt A0A2D2BEZ7
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