1RIN
X-RAY CRYSTAL STRUCTURE OF A PEA LECTIN-TRIMANNOSIDE COMPLEX AT 2.6 ANGSTROMS RESOLUTION
- PDB DOI: https://doi.org/10.2210/pdb1RIN/pdb
- Classification: LECTIN
- Organism(s): Pisum sativum
- Mutation(s): No
- Deposited: 1993-01-27 Released: 1993-10-31
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Work: 0.183
- R-Value Observed: 0.183
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 |
| PEA LECTIN | 180 | Pisum sativum | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for P02867 (Pisum sativum) Explore P02867 Go to UniProtKB: P02867 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P02867 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| PEA LECTIN | 49 | Pisum sativum | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for P02867 (Pisum sativum) Explore P02867 Go to UniProtKB: P02867 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P02867 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| MAN Query on MAN | E [auth A], H [auth C] | alpha-D-mannopyranose C6 H12 O6 WQZGKKKJIJFFOK-PQMKYFCFSA-N |  | ||
| MN Query on MN | F [auth A], I [auth C] | MANGANESE (II) ION Mn WAEMQWOKJMHJLA-UHFFFAOYSA-N |  | ||
| CA Query on CA | G [auth A], J [auth C] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Work: 0.183
- R-Value Observed: 0.183
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 64.3 | α = 90 |
| b = 73.4 | β = 90 |
| c = 108.5 | γ = 90 |
| Software Name | Purpose |
|---|---|
| X-PLOR | model building |
| X-PLOR | refinement |
| X-PLOR | phasing |
Entry History
Deposition Data
- Released Date: 1993-10-31 Deposition Author(s): Rini, J.M., Hardman, K.D., Einspahr, H., Suddath, F.L., Carver, J.P.
Revision History (Full details and data files)
- Version 1.0: 1993-10-31
Type: Initial release - Version 1.1: 2008-03-24
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Derived calculations, Version format compliance - Version 1.3: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Database references, Derived calculations, Other, Structure summary - Version 1.4: 2024-02-14
Changes: Data collection, Database references, Structure summary
