4CAD
Mechanism of farnesylated CAAX protein processing by the integral membrane protease Rce1
- PDB DOI: https://doi.org/10.2210/pdb4CAD/pdb
- Classification: PROTEIN BINDING
- Organism(s): Mus musculus, Methanococcus maripaludis
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No 
- Membrane Protein: Yes  OPMPDBTMMemProtMDmpstruc
- Deposited: 2013-10-08 Released: 2013-11-27 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.267 
- R-Value Work: 0.226 
- R-Value Observed: 0.228 
This is version 1.5 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 |
ANTIBODY FAB FRAGMENT LIGHT CHAIN | 214 | Mus musculus | Mutation(s): 0  | ||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
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 |
ANTIBODY FAB FRAGMENT HEAVY CHAIN | 227 | Mus musculus | Mutation(s): 0  | ||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
|
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 3 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
RAS AND A-FACTOR CONVERTING ENZYME 1, RCE1 | 271 | Methanococcus maripaludis | Mutation(s): 0  Membrane Entity: Yes  | ||
UniProt | |||||
Find proteins for Q6LZY8 (Methanococcus maripaludis (strain S2 / LL)) Explore Q6LZY8  Go to UniProtKB:  Q6LZY8 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q6LZY8 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
Ligands 2 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
LMT Query on LMT | O [auth I], P [auth L] | DODECYL-BETA-D-MALTOSIDE C24 H46 O11 NLEBIOOXCVAHBD-QKMCSOCLSA-N | |||
BOG Query on BOG | M [auth C], N [auth F] | octyl beta-D-glucopyranoside C14 H28 O6 HEGSGKPQLMEBJL-RKQHYHRCSA-N |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.267 
- R-Value Work: 0.226 
- R-Value Observed: 0.228 
- Space Group: P 1
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 113.063 | α = 89.06 |
b = 90.087 | β = 102.29 |
c = 99.3 | γ = 90 |
Software Name | Purpose |
---|---|
PHENIX | refinement |
XDS | data reduction |
SCALA | data scaling |
PHASER | phasing |
Entry History 
Deposition Data
- Released Date: 2013-11-27  Deposition Author(s): Kulkarni, K., Manolaridis, I., Dodd, R.B., Cronin, N., Ogasawara, S., Iwata, S., Barford, D.
Revision History (Full details and data files)
- Version 1.0: 2013-11-27
Type: Initial release - Version 1.1: 2013-12-11
Changes: Database references - Version 1.2: 2013-12-18
Changes: Database references - Version 1.3: 2018-01-24
Changes: Source and taxonomy - Version 1.4: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Other, Structure summary - Version 1.5: 2023-12-20
Changes: Data collection, Database references, Refinement description, Structure summary