Download MendeleyCrystal Structure of the Catalytic Domain of MCR-1 (cMCR-1) in Complex with d-Xylose
Liu, Z.X., Han, Z., Yu, X.L., Wen, G., Zeng, C.(2018) Crystals (Basel) 8
5ZJV
Crystal structure of the catalytic domain of MCR-1 (cMCR-1) in complex with xylose
- PDB DOI: https://doi.org/10.2210/pdb5ZJV/pdb
- Classification: TRANSFERASE
- Organism(s): Escherichia coli
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2018-03-22 Released: 2018-04-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.82 Å
- R-Value Free: 0.186
- R-Value Work: 0.148
- R-Value Observed: 0.150
Starting Model: experimental
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This is version 1.3 of the entry. See complete history.
Literature
Macromolecules
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(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Probable phosphatidylethanolamine transferase Mcr-1 | 331 | Escherichia coli | Mutation(s): 0 Gene Names: mcr1, mcr-1, APZ14_31440 EC: 2.7 |  | |
UniProt | |||||
Find proteins for A0A0R6L508 (Escherichia coli) Explore A0A0R6L508 Go to UniProtKB: A0A0R6L508 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A0R6L508 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| LXC Query on LXC | B [auth A] | beta-L-xylopyranose C5 H10 O5 SRBFZHDQGSBBOR-QTBDOELSSA-N |  | ||
| ZN Query on ZN | C [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| TPO Query on TPO | A | L-PEPTIDE LINKING | C4 H10 N O6 P |  | THR |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.82 Å
- R-Value Free: 0.186
- R-Value Work: 0.148
- R-Value Observed: 0.150
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 51.58 | α = 90 |
| b = 73.13 | β = 90 |
| c = 82.3 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| iMOSFLM | data reduction |
| SCALA | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
Revision History (Full details and data files)
- Version 1.0: 2018-04-25
Type: Initial release - Version 1.1: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Structure summary - Version 1.2: 2023-11-22
Changes: Advisory, Data collection, Database references, Refinement description, Structure summary - Version 1.3: 2024-11-20
Changes: Structure summary
