MolNFT v1 · #184008 · protein
Conserved hypothetical protein residues 311-335 from candidatus magnetomorum sp. hk-1 fused to GCN4 adaptors, mutant BETA1/A, crystal form III
7OAF · General control transcription factor GCN4,CONSERVED…: “Conserved hypothetical protein residues 311-335 from candidatus magnetomorum sp. hk-1 fused to GCN4 adaptors…”. X-ray diffraction. MolNFT v1 #184008 on GenesisL1: 3D structure…
- PDB
- 7OAF
- Type
- protein
- Length
- 243 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- General control transcription factor GCN4,CONSERVED hypothetical protein residues 311-335…
- UniProt
- P03069, A0A0N0D484
Structure
x-ray diffraction · 1 distinct chain · 77% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | General control transcription factor GCN4,CONSERVED hypothetical protein residues 311-335 from candidatus magnetomorum sp. hk-1 fused to GCN4 adaptors, mutant BETA1/A,GENERAL control transcription factor GCN4 | protein | 81 | 77% helix, 2% strand | P03069, A0A0N0D484 |
Ligands and binding sites
- 1PE · Pentaethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1866 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 1832 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1775 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7OAF · conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1… · the same entry in another collection · chain A against A, TM-score 1.00
- P03069 · AlphaFold monomer V2.0 prediction for general control transcription factor GCN4 (P03069) · a predicted model of the same protein · chain A against A, TM-score 0.44
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 P03069
- Every structure of UniProt A0A0N0D484
- Elsewhere: RCSB PDB 7OAF · PDBe 7OAF · UniProt P03069 · UniProt A0A0N0D484
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