MolNFT v1 · #156971 · protein
Crystallographic solvent mapping analysis of DMSO/MG bound to APE1
6MKK: “Crystallographic solvent mapping analysis of DMSO/MG bound to APE1”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #156971 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6MKK
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P27695
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 282 | — | P27695 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6MKK · Crystallographic solvent mapping analysis of DMSO/Mg bound to APE1 · the same entry in another collection · chain A against A, TM-score 1.00
- P27695 · AlphaFold monomer V2.0 prediction for DNA-(apurinic or apyrimidinic site) endonuclease… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P27695
- Elsewhere: RCSB PDB 6MKK · PDBe 6MKK · UniProt P27695
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