MolNFT v1 · #15964 · protein + DNA
Crystal structure of myc-max recognizing DNA
1NKP: “Crystal structure of myc-max recognizing DNA”. X-ray diffraction. MolNFT v1 #15964 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NKP
- Type
- protein + DNA
- Length
- 411 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01106, P61244
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, G, H, J | — | dna | 19 | — | — |
| A | — | protein | 88 | — | P01106 |
| B | — | protein | 83 | — | P61244 |
| D | — | protein | 83 | — | P01106 |
| E | — | protein | 81 | — | P61244 |
Compared structures
- 1NKP · Crystal structure of Myc-Max recognizing DNA · the same entry in another collection · chain E against E, TM-score 1.00
- P61244 · AlphaFold monomer V2.0 prediction for protein max (P61244) · a predicted model of the same protein · chain B against A, TM-score 0.96
- P01106 · AlphaFold monomer V2.0 prediction for myc proto-oncogene protein (P01106) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P01106
- Every structure of UniProt P61244
- Elsewhere: RCSB PDB 1NKP · PDBe 1NKP · UniProt P01106 · UniProt P61244
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