Download MendeleyStructure of human hydroxyacid oxidase 1 bound with FMN and glycolate
MacKinnon, S., Bezerra, G.A., Krojer, T., Smee, C., Arrowsmith, C.H., Edwards, E., Bountra, C., Oppermann, U., Brennan, P.E., Yue, W.W.To be published.
6GMC
1.2 A resolution structure of human hydroxyacid oxidase 1 bound with FMN and 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole
- PDB DOI: https://doi.org/10.2210/pdb6GMC/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2018-05-24 Released: 2018-06-13
- Funding Organization(s): Wellcome Trust
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.20 Å
- R-Value Free: 0.155
- R-Value Work: 0.134
- R-Value Observed: 0.135
This is version 2.1 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 |
| Hydroxyacid oxidase 1 | 368 | Homo sapiens | Mutation(s): 0 Gene Names: HAO1, GOX1, HAOX1 EC: 1.1.3.15 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q9UJM8 (Homo sapiens) Explore Q9UJM8 Go to UniProtKB: Q9UJM8 | |||||
PHAROS: Q9UJM8 GTEx: ENSG00000101323 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9UJM8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FMN Query on FMN | F [auth A] | FLAVIN MONONUCLEOTIDE C17 H21 N4 O9 P FVTCRASFADXXNN-SCRDCRAPSA-N |  | ||
| C7C Query on C7C | G [auth A] | 5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole-4-carboxylate C9 H4 Cl N2 O2 S2 NDYKFFAREALEPX-UHFFFAOYSA-M |  | ||
| EDO Query on EDO | B [auth A], C [auth A], D [auth A], E [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.20 Å
- R-Value Free: 0.155
- R-Value Work: 0.134
- R-Value Observed: 0.135
- Space Group: I 4
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 97.348 | α = 90 |
| b = 97.348 | β = 90 |
| c = 80.363 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SCALA | data scaling |
| PDB_EXTRACT | data extraction |
| SCALA | data scaling |
| PHASER | phasing |
| XDS | data reduction |
Entry History & Funding Information
Deposition Data
- Released Date: 2018-06-13 Deposition Author(s): MacKinnon, S., Bezerra, G.A., Krojer, T., Smee, C., Arrowsmith, C.H., Edwards, E., Bountra, C., Oppermann, U., Brennan, P.E., Yue, W.W.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Wellcome Trust | United Kingdom | 106169/ZZ14/Z |
Revision History (Full details and data files)
- Version 1.0: 2018-06-13
Type: Initial release - Version 2.0: 2018-06-27
Changes: Atomic model, Data collection, Derived calculations - Version 2.1: 2024-01-17
Changes: Data collection, Database references, Refinement description
