Research workbench
Crystal structure of HOPZ1A in complex with IP6 and CoA
Analyse Crystal structure of HOPZ1A in complex with IP6 and CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KLQ
- Type
- protein
- Length
- 964 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6VE93
- Ligands
- IHP, COA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, B | — | protein | 320 | — | Q6VE93 |
| A | — | protein | 324 | — | Q6VE93 |
Ligands and binding sites
- IHP · Inositol hexakisphosphate · ligand · 3 copies · chains C, A, B
- COA · Coenzyme A · ligand · 3 copies · chains C, A, B
- CIT · Citric acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5KLQ · Crystal structure of HopZ1a in complex with IP6 and CoA · the same entry in another collection · chain C against C, TM-score 1.00
- Q6VE93 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein acetyltransferase HOPZ1A… · a predicted model of the same protein · chain C against A, TM-score 0.97
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 Q6VE93
- Elsewhere: RCSB PDB 5KLQ · PDBe 5KLQ · UniProt Q6VE93
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.