MolNFT v1 · #168271 · protein
Complex structure of PHF19
6WAU: “Complex structure of PHF19”. X-ray diffraction, 1 ligand (UNX). MolNFT v1 #168271 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6WAU
- Type
- protein
- Length
- 385 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5T6S3, Q16695
- Ligands
- UNX
Structure
x-ray diffraction · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 57 | — | Q5T6S3 |
| B | — | protein | 56 | — | Q5T6S3 |
| C | — | protein | 56 | — | Q5T6S3 |
| D, F | — | protein | 55 | — | Q5T6S3 |
| E | — | protein | 52 | — | Q5T6S3 |
| G, H, J, K | — | protein | 9 | — | Q16695 |
| I | — | protein | 10 | — | Q16695 |
| L | — | protein | 8 | — | Q16695 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 11 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6WAU · Complex structure of PHF19 · the same entry in another collection · chain L against L, TM-score 1.00
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 Q5T6S3
- Every structure of UniProt Q16695
- Elsewhere: RCSB PDB 6WAU · PDBe 6WAU · UniProt Q5T6S3 · UniProt Q16695
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