Download MendeleyStructural and Biochemical Characterization of the Human Blood Group a and B Galactosyltransferases Possessing the Pro156Leu Mutation
Weadge, J., Palcic, M.M., Henriksen, A.To be published.
2Y7A | pdb_00002y7a
Crystal structure of unliganded GTB P156L
- PDB DOI: https://doi.org/10.2210/pdb2Y7A/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2011-01-31 Released: 2012-02-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.06 Å
- R-Value Free: 0.245 (Depositor), 0.250 (DCC)
- R-Value Work: 0.216 (Depositor), 0.220 (DCC)
- R-Value Observed: 0.217 (Depositor)
Starting Model: experimental
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This is version 1.3 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 |
| ABO GLYCOSYLTRANSFERASE | 298 | Homo sapiens | Mutation(s): 1 EC: 2.4.1.37 (PDB Primary Data), 2.4.1.40 (UniProt) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P16442 (Homo sapiens) Explore P16442 Go to UniProtKB: P16442 | |||||
PHAROS: P16442 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P16442 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| UDP Query on UDP | F [auth A] | URIDINE-5'-DIPHOSPHATE C9 H14 N2 O12 P2 XCCTYIAWTASOJW-XVFCMESISA-N |  | ||
| MN Query on MN | E [auth A] | MANGANESE (II) ION Mn WAEMQWOKJMHJLA-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.06 Å
- R-Value Free: 0.245 (Depositor), 0.250 (DCC)
- R-Value Work: 0.216 (Depositor), 0.220 (DCC)
- R-Value Observed: 0.217 (Depositor)
Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 63.73 | α = 90 |
| b = 78.29 | β = 88.96 |
| c = 143.74 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| MOSFLM | data reduction |
| SCALA | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2012-02-15 Deposition Author(s): Weadge, J., Palcic, M.M., Henriksen, A.
Revision History (Full details and data files)
- Version 1.0: 2012-02-15
Type: Initial release - Version 1.1: 2012-10-03
Changes: Derived calculations - Version 1.2: 2017-07-12
Changes: Data collection - Version 1.3: 2023-12-20
Changes: Data collection, Database references, Derived calculations, Other, Refinement description
