Download MendeleyAspH-H679A.Factor X Complex
Pfeffer, I., Chowdhury, R., Schofield, C.J.To be published.
6Q9I
Aspartyl/Asparaginyl beta-hydroxylase (AspH) H679A in complex with Factor X peptide fragment (39mer-4Ser)
- PDB DOI: https://doi.org/10.2210/pdb6Q9I/pdb
- Classification: GENE REGULATION
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2018-12-18 Released: 2020-01-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.223
- R-Value Work: 0.202
- R-Value Observed: 0.203
Starting Model: experimental
View more details
wwPDB Validation 3D Report Full Report
This is version 1.2 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Aspartyl/asparaginyl beta-hydroxylase | 429 | Homo sapiens | Mutation(s): 1 Gene Names: ASPH, BAH EC: 1.14.11.16 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q12797 (Homo sapiens) Explore Q12797 Go to UniProtKB: Q12797 | |||||
PHAROS: Q12797 GTEx: ENSG00000198363 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q12797 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Coagulation factor X | 39 | Homo sapiens | Mutation(s): 4 EC: 3.4.21.6 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P00742 (Homo sapiens) Explore P00742 Go to UniProtKB: P00742 | |||||
PHAROS: P00742 GTEx: ENSG00000126218 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P00742 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | E [auth A], F [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| FMT Query on FMT | C [auth A], D [auth A], G [auth B] | FORMIC ACID C H2 O2 BDAGIHXWWSANSR-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.223
- R-Value Work: 0.202
- R-Value Observed: 0.203
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 50.125 | α = 90 |
| b = 91.359 | β = 90 |
| c = 123.538 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2020-01-15 Deposition Author(s): Chowdhury, R., Pfeffer, I., Schofield, C.J.
Revision History (Full details and data files)
- Version 1.0: 2020-01-15
Type: Initial release - Version 1.1: 2024-01-24
Changes: Data collection, Database references, Refinement description - Version 1.2: 2024-10-09
Changes: Structure summary
