MolNFT v1 · #131883 · protein
Pandda analysis group deposition of models with modelled events (E.G. bound ligands) -- crystal structure of NUDT7 in complex with RK4-337
5QHC: “Pandda analysis group deposition of models with modelled events (E.G. bound ligands) -- crystal structure of…”. X-ray diffraction, 1 ligand (H2M). MolNFT v1 #131883 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5QHC
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0C024
- Ligands
- H2M
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 186 | — | P0C024 |
Ligands and binding sites
- H2M · 1-[3'-(trifluoromethyl)[1,1'-biphenyl]-2-yl]-1,3-dihydro-2H-pyrrol-2-one · ligand · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- DMS · Dimethyl sulfoxide · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P0C024 · AlphaFold monomer V2.0 prediction for peroxisomal coenzyme a diphosphatase NUDT7 (P0C024) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P0C024
- Elsewhere: RCSB PDB 5QHC · PDBe 5QHC · UniProt P0C024
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