MolNFT v1 · #183074 · protein + DNA
Human TET2 in complex with favourable DNA substrate.
7NE3: “Human TET2 in complex with favourable DNA substrate.”. X-ray diffraction, 3 ligands (OGA, ZN, FE2). MolNFT v1 #183074 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7NE3
- Type
- protein + DNA
- Length
- 439 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6N021
- Ligands
- OGA, ZN, FE2
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 416 | — | Q6N021 |
| B | — | dna | 11 | — | — |
| C | — | dna | 12 | — | — |
Ligands and binding sites
- OGA · N-oxalylglycine · ligand · chains A, B
- ZN · Zinc ion · metal · 3 copies · chains A
- FE2 · Fe (II) ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, C, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q6N021
- Elsewhere: RCSB PDB 7NE3 · PDBe 7NE3 · UniProt Q6N021
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