MolNFT v1 · #160230 · protein
Crystal structure of HEMK2-TRMT112 complex
6PED: “Crystal structure of HEMK2-TRMT112 complex”. X-ray diffraction, 1 ligand (UNX). MolNFT v1 #160230 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PED
- Type
- protein
- Length
- 320 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9Y5N5, Q9UI30
- Ligands
- UNX
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 194 | — | Q9Y5N5 |
| B | — | protein | 126 | — | Q9UI30 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 12 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PED · Crystal structure of HEMK2-TRMT112 complex · the same entry in another collection · chain B against B, TM-score 1.00
- Q9Y5N5 · AlphaFold monomer V2.0 prediction for methyltransferase N6AMT1 (Q9Y5N5) · a predicted model of the same protein · chain A against A, TM-score 0.98
- Q9UI30 · AlphaFold monomer V2.0 prediction for multifunctional methyltransferase subunit… · a predicted model of the same protein · chain B against A, TM-score 0.94
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 Q9Y5N5
- Every structure of UniProt Q9UI30
- Elsewhere: RCSB PDB 6PED · PDBe 6PED · UniProt Q9Y5N5 · UniProt Q9UI30
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