Download MendeleyCryo-EM structure of human lanosterol 14alpha-demethylase (CYP51) in complex with FLZ
Zhou, L.C.To be published.
8YQO | pdb_00008yqo
Cryo-EM structure of human lanosterol 14alpha-demethylase (CYP51) in complex with FLZ
- PDB DOI: https://doi.org/10.2210/pdb8YQO/pdb
- EM Map EMD-39501: EMDB EMDataResource
- Classification: PROTEIN BINDING
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2024-03-19 Released: 2025-03-26
- Funding Organization(s): National Natural Science Foundation of China (NSFC)
Experimental Data Snapshot
- Method: ELECTRON MICROSCOPY
- Resolution: 3.52 Å
- Aggregation State: PARTICLE
- Reconstruction Method: SINGLE PARTICLE
wwPDB Validation 3D Report Full Report
This is version 1.0 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Lanosterol 14-alpha demethylase | 458 | Homo sapiens | Mutation(s): 0 Gene Names: CYP51A1, CYP51 EC: 1.14.14.154 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q16850 (Homo sapiens) Explore Q16850 Go to UniProtKB: Q16850 | |||||
PHAROS: Q16850 GTEx: ENSG00000001630 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q16850 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| HEM (Subject of Investigation/LOI) Query on HEM | B [auth A] | PROTOPORPHYRIN IX CONTAINING FE C34 H32 Fe N4 O4 KABFMIBPWCXCRK-RGGAHWMASA-L |  | ||
| A1D61 (Subject of Investigation/LOI) Query on A1D61 | C [auth A] | (~{E})-2-(2,5-dimethoxyphenyl)-~{N}-[2-(4-hydroxyphenyl)ethyl]-3-(3-methoxy-4-oxidanyl-phenyl)prop-2-enamide C26 H27 N O6 ZZTHOXZXWINLQI-HYARGMPZSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: ELECTRON MICROSCOPY
- Resolution: 3.52 Å
- Aggregation State: PARTICLE
- Reconstruction Method: SINGLE PARTICLE
Entry History & Funding Information
Deposition Data
- Released Date: 2025-03-26 Deposition Author(s): Zhou, L.C.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Natural Science Foundation of China (NSFC) | China | -- |
Revision History (Full details and data files)
- Version 1.0: 2025-03-26
Type: Initial release
