1W2K
tf7a_4380 complex
- PDB DOI: https://doi.org/10.2210/pdb1W2K/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Mesocricetus auratus, Escherichia coli
- Mutation(s): No 
- Deposited: 2004-07-06 Released: 2005-06-20 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 3.00 Å
- R-Value Free: 0.257 
- R-Value Work: 0.197 
wwPDB Validation   3D Report Full Report
This is version 1.4 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 |
BLOOD COAGULATION FACTOR VIIA | A [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 | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
BLOOD COAGULATION FACTOR VIIA | B [auth L] | 142 | 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 | |||||
|
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 3 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
TISSUE FACTOR | C [auth T] | 210 | Homo sapiens | Mutation(s): 0  | |
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 | |||||
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Small Molecules
Ligands 5 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
380 Query on 380 | D [auth H] | (2R)-2-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO)-N-BENZYL-2-(3,4-DIMETHOXYPHENYL)ACETAMIDE C24 H26 N4 O3 BMQMRSICTKGCCO-JOCHJYFZSA-N | |||
BGC Query on BGC | P [auth L] | beta-D-glucopyranose C6 H12 O6 WQZGKKKJIJFFOK-VFUOTHLCSA-N | |||
FUC Query on FUC | G [auth L] | alpha-L-fucopyranose C6 H12 O5 SHZGCJCMOBCMKK-SXUWKVJYSA-N | |||
CAC Query on CAC | F [auth H] | CACODYLATE ION C2 H6 As O2 OGGXGZAMXPVRFZ-UHFFFAOYSA-M | |||
CA Query on CA | E [auth H] H [auth L] I [auth L] J [auth L] K [auth L] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |
Modified Residues 1 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Type | Formula | 2D Diagram | Parent |
CGU Query on CGU | B [auth L] | L-PEPTIDE LINKING | C6 H9 N O6 | GLU |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 3.00 Å
- R-Value Free: 0.257 
- R-Value Work: 0.197 
- Space Group: P 21 21 21
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 71.874 | α = 90 |
b = 82.638 | β = 90 |
c = 123.722 | γ = 90 |
Software Name | Purpose |
---|---|
CNX | refinement |
XDS | data reduction |
XDS | data scaling |
Entry History 
Deposition Data
- Released Date: 2005-06-20  Deposition Author(s): Banner, D.W., D'Arcy, A., Groebke-Zbinden, K., Ackermann, J., Kirchhofer, D., Ji, Y.-H., Tschopp, T.B., Wallbaum, S., Weber, L.
Revision History (Full details and data files)
- Version 1.0: 2005-06-20
Type: Initial release - Version 1.1: 2011-05-08
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Data collection, Derived calculations, Other, Structure summary - Version 1.4: 2023-12-13
Changes: Advisory, Data collection, Database references, Refinement description, Structure summary