Download MendeleyHuman factor viia-tissue factor complexed with highly selective peptide inhibitor
Kadono, S., Sakamoto, A., Kikuchi, Y., Oh-Eda, M., Yabuta, N., Koga, T., Hattori, K., Shiraishi, T., Haramura, M., Sato, H., Ohta, M., Kozono, T.To be published.
2ZWL
Human factor viia-tissue factor complexed with highly selective peptide inhibitor
- PDB DOI: https://doi.org/10.2210/pdb2ZWL/pdb
- Classification: HYDROLASE/BLOOD CLOTTING
- Organism(s): Homo sapiens
- Expression System: Cricetulus griseus, Escherichia coli
- Mutation(s): No
- Deposited: 2008-12-16 Released: 2009-01-20
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.267
- R-Value Work: 0.226
This is version 1.4 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 |
| Factor VII light chain | A [auth L] | 152 | Homo sapiens | Mutation(s): 0 Gene Names: F7 EC: 3.4.21.21 |  |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P08709 (Homo sapiens) Explore P08709 Go to UniProtKB: P08709 | |||||
PHAROS: P08709 GTEx: ENSG00000057593 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P08709 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Factor VII heavy chain | B [auth H] | 254 | Homo sapiens | Mutation(s): 0 Gene Names: F7 EC: 3.4.21.21 |  |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P08709 (Homo sapiens) Explore P08709 Go to UniProtKB: P08709 | |||||
PHAROS: P08709 GTEx: ENSG00000057593 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P08709 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 3 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Tissue factor | C [auth T] | 218 | Homo sapiens | Mutation(s): 0 Gene Names: F3 |  |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P13726 (Homo sapiens) Explore P13726 Go to UniProtKB: P13726 | |||||
PHAROS: P13726 GTEx: ENSG00000117525 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P13726 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 567 Query on 567 | N [auth H] | 2-[[(2R)-1-[[(2S)-5-amino-1-[(4-carbamimidoylphenyl)methylamino]-1,5-dioxo-pentan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxo-propan-2-yl]sulfamoyl]ethanoic acid C26 H31 N7 O7 S NLKRKTGGXZDTOO-LEWJYISDSA-N |  | ||
| BGC Query on BGC | D [auth L] | beta-D-glucopyranose C6 H12 O6 WQZGKKKJIJFFOK-VFUOTHLCSA-N |  | ||
| FUC Query on FUC | E [auth L] | alpha-L-fucopyranose C6 H12 O5 SHZGCJCMOBCMKK-SXUWKVJYSA-N |  | ||
| CA Query on CA | F [auth L] G [auth L] H [auth L] I [auth L] J [auth L] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| CGU Query on CGU | A [auth L] | L-PEPTIDE LINKING | C6 H9 N O6 |  | GLU |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.267
- R-Value Work: 0.226
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 71.4 | α = 90 |
| b = 82.22 | β = 90 |
| c = 123.47 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| DENZO | data reduction |
| SCALEPACK | data scaling |
| CNS | phasing |
Entry History
Deposition Data
- Released Date: 2009-01-20 Deposition Author(s): Kadono, S., Sakamoto, A., Kikuchi, Y., Oh-Eda, M., Yabuta, N., Koga, T., Hattori, K., Shiraishi, T., Haramura, M., Sato, H., Ohta, M., Kozono, T.
Revision History (Full details and data files)
- Version 1.0: 2009-01-20
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Data collection, Derived calculations, Structure summary - Version 1.3: 2023-11-01
Changes: Advisory, Data collection, Database references, Refinement description, Structure summary - Version 1.4: 2023-11-15
Changes: Data collection
