1DZH
P14-FLUORESCEIN-N135Q-S380C-ANTITHROMBIN-III
- PDB DOI: https://doi.org/10.2210/pdb1DZH/pdb
- Classification: BLOOD CLOTTING
- Organism(s): Homo sapiens
- Expression System: Cricetinae gen. sp.
- Mutation(s): Yes 
- Deposited: 2000-02-28 Released: 2000-05-26 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.85 Å
- R-Value Free: 0.258 
- R-Value Work: 0.207 
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 |
ANTITHROMBIN-III | A [auth I] | 432 | Homo sapiens | Mutation(s): 2  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01008 (Homo sapiens) Explore P01008  Go to UniProtKB:  P01008 | |||||
PHAROS:  P01008 GTEx:  ENSG00000117601  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P01008 | ||||
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 |
ANTITHROMBIN-III | B [auth L] | 432 | Homo sapiens | Mutation(s): 0  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P01008 (Homo sapiens) Explore P01008  Go to UniProtKB:  P01008 | |||||
PHAROS:  P01008 GTEx:  ENSG00000117601  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P01008 | ||||
Sequence AnnotationsExpand | |||||
|
Oligosaccharides
Entity ID: 3 | |||||
---|---|---|---|---|---|
Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | C [auth A], D [auth B] | 2 | N-Glycosylation | ||
Glycosylation Resources | |||||
GlyTouCan:  G42666HT GlyCosmos:  G42666HT GlyGen:  G42666HT |
Entity ID: 4 | |||||
---|---|---|---|---|---|
Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | E [auth C] | 4 | N-Glycosylation | ||
Glycosylation Resources | |||||
GlyTouCan:  G31886NL GlyCosmos:  G31886NL GlyGen:  G31886NL |
Small Molecules
Ligands 2 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
NAG Query on NAG | F [auth I], G [auth I], I [auth L] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N | |||
GOL Query on GOL | H [auth I], J [auth L] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |
Modified Residues 1 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Type | Formula | 2D Diagram | Parent |
CYF Query on CYF | A [auth I] | L-PEPTIDE LINKING | C25 H23 N3 O7 S | CYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.85 Å
- R-Value Free: 0.258 
- R-Value Work: 0.207 
- Space Group: P 1 21 1
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 69.175 | α = 90 |
b = 99.865 | β = 105.63 |
c = 89.421 | γ = 90 |
Software Name | Purpose |
---|---|
REFMAC | refinement |
MOSFLM | data reduction |
SCALA | data scaling |
AMoRE | phasing |
Entry History 
Deposition Data
- Released Date: 2000-05-26  Deposition Author(s): Mccoy, A.J., Huntington, J.A., Carrell, R.W.
Revision History (Full details and data files)
- Version 1.0: 2000-05-26
Type: Initial release - Version 1.1: 2011-05-26
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2017-07-12
Changes: Advisory - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Derived calculations, Other, Structure summary - Version 2.1: 2023-12-06
Changes: Data collection, Database references, Derived calculations, Refinement description, Structure summary