1NMU
MBP-L30
- PDB DOI: https://doi.org/10.2210/pdb1NMU/pdb
- Classification: SUGAR BINDING PROTEIN/RIBOSOME
- Organism(s): Escherichia coli, Saccharomyces cerevisiae
- Expression System: Escherichia coli, Saccharomyces cerevisiae
- Mutation(s): No 
- Deposited: 2003-01-10 Released: 2003-02-18 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.31 Å
- R-Value Free: 0.254 
- R-Value Work: 0.214 
- R-Value Observed: 0.223 
wwPDB Validation   3D Report Full Report
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 |
maltose-binding periplasmic protein | 382 | Escherichia coli | Mutation(s): 0  | ||
UniProt | |||||
Find proteins for P0AEX9 (Escherichia coli (strain K12)) Explore P0AEX9  Go to UniProtKB:  P0AEX9 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P0AEX9 | ||||
Sequence AnnotationsExpand | |||||
|
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
60S ribosomal protein L30 | 104 | Saccharomyces cerevisiae | Mutation(s): 0  | ||
UniProt | |||||
Find proteins for P14120 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P14120  Go to UniProtKB:  P14120 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P14120 | ||||
Sequence AnnotationsExpand | |||||
|
Oligosaccharides
Biologically Interesting Molecules (External Reference) 1 Unique
Entity ID: 3 | |||||
---|---|---|---|---|---|
ID | Chains | Name | Type/Class | 2D Diagram | 3D Interactions |
PRD_900010 Query on PRD_900010 | E, F | alpha-maltotetraose | Oligosaccharide / Substrate analog |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.31 Å
- R-Value Free: 0.254 
- R-Value Work: 0.214 
- R-Value Observed: 0.223 
- Space Group: P 21 21 21
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 79.65 | α = 90 |
b = 118.39 | β = 90 |
c = 153.78 | γ = 90 |
Software Name | Purpose |
---|---|
MOSFLM | data reduction |
SCALA | data scaling |
AMoRE | phasing |
CNS | refinement |
CCP4 | data scaling |
Entry History 
Deposition Data
- Released Date: 2003-02-18  Deposition Author(s): Chao, J.A., Prasad, G.S., White, S.A., Stout, C.D., Williamson, J.R.
Revision History (Full details and data files)
- Version 1.0: 2003-02-18
Type: Initial release - Version 1.1: 2008-04-29
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Non-polymer description, Structure summary - Version 2.1: 2022-12-21
Changes: Database references, Structure summary