1QFK
STRUCTURE OF HUMAN FACTOR VIIA AND ITS IMPLICATIONS FOR THE TRIGGERING OF BLOOD COAGULATION
- PDB DOI: https://doi.org/10.2210/pdb1QFK/pdb
- Classification: hydrolase/hydrolase inhibitor
- Organism(s): Homo sapiens
- Expression System: Mesocricetus auratus
- Mutation(s): No 
- Deposited: 1999-04-12 Released: 1999-08-01 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.80 Å
- R-Value Free: 0.267 
- R-Value Work: 0.215 
This is version 2.1 of the entry. See complete history. 
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
COAGULATION FACTOR VIIA LIGHT CHAIN | A [auth L] | 104 | Homo sapiens | Mutation(s): 0  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 | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
COAGULATION FACTOR VIIA HEAVY CHAIN | B [auth H] | 254 | Homo sapiens | Mutation(s): 0  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 | |||||
|
Oligosaccharides
Entity ID: 3 | |||||
---|---|---|---|---|---|
Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | C [auth A] | 3 | N-Glycosylation | ||
Glycosylation Resources | |||||
GlyTouCan:  G28454KX GlyCosmos:  G28454KX GlyGen:  G28454KX |
Small Molecules
Ligands 4 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
0Z6 Query on 0Z6 | F [auth H] | D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-phenylalaninamide C25 H36 Cl N6 O3 ZKHBINZTIMXMQW-CLAROIROSA-O | |||
GLC Query on GLC | D [auth L] | alpha-D-glucopyranose C6 H12 O6 WQZGKKKJIJFFOK-DVKNGEFBSA-N | |||
FUC Query on FUC | E [auth L] | alpha-L-fucopyranose C6 H12 O5 SHZGCJCMOBCMKK-SXUWKVJYSA-N | |||
CA Query on CA | G [auth H] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |
Biologically Interesting Molecules (External Reference) 1 Unique
Entity ID: 6 | |||||
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ID | Chains | Name | Type/Class | 2D Diagram | 3D Interactions |
PRD_000369 (0Z6) Query on PRD_000369 | F [auth H] | D-Phe-Phe-Arg Chloromethylketone | Peptide-like / Inhibitor |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.80 Å
- R-Value Free: 0.267 
- R-Value Work: 0.215 
- Space Group: P 43 2 2
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 115.3 | α = 90 |
b = 115.3 | β = 90 |
c = 98 | γ = 90 |
Software Name | Purpose |
---|---|
DENZO | data reduction |
SCALEPACK | data scaling |
AMoRE | phasing |
REFMAC | refinement |
Entry History 
Deposition Data
- Released Date: 1999-08-01  Deposition Author(s): Pike, A.C.W., Brzozowski, A.M., Roberts, S.M., Olsen, O.H., Persson, E.
Revision History (Full details and data files)
- Version 1.0: 1999-08-01
Type: Initial release - Version 1.1: 2007-10-16
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Atomic model, Database references, Derived calculations, Non-polymer description, Structure summary, Version format compliance - Version 1.3: 2012-12-12
Changes: Other - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Derived calculations, Structure summary - Version 2.1: 2023-08-16
Changes: Data collection, Database references, Refinement description, Structure summary