Detail Information of Inter-species Structural Difference

General Information of Drug Transporter (DT)
DT ID DTD0060 Transporter Info
Gene Name ABCC7
Protein Name Cystic fibrosis transmembrane conductance regulator
Gene ID
1080
UniProt ID
P13569
3D Structure

Crystal Structure of This DT

Crystallisation Method:EM

PDB ID:5UAK

Corresponding Chain:A

Sequence Length:1-1480

Detail: Struture Info

Inter-species Structural Differences (ISD)
Mus musculus (Mouse)
        Gene Name Cftr
        UniProt ID
P26361
        UniProt Entry
CFTR_MOUSE
        3D Structure

Crystallisation Method:X-ray

Expression System:Escherichia coli

PDB ID:1R0W

Corresponding Chain:A/B/C/D

Sequence Length:389-673
Click to Save PDB File in PDB Format
        Experimental Structures of This Model Oganism
                PDB ID Scanning Method Resolution Expression System Details Ref
                1Q3H X-ray 2.5 Å Escherichia coli
Click to Show/Hide the Details
[ 1]
Structure
Click to Save PDB File in TXT Format
Corresponding chain A/B/C/D
Sequence Length 389-673 Mutation No
                1R0X X-ray 2.2 Å Escherichia coli
Click to Show/Hide the Details
[ 1]
Structure
Click to Save PDB File in TXT Format
Corresponding chain A/B/C/D
Sequence Length 389-673 Mutation No
                1R0Y X-ray 2.55 Å Escherichia coli
Click to Show/Hide the Details
[ 1]
Structure
Click to Save PDB File in TXT Format
Corresponding chain A/B/C/D
Sequence Length 389-673 Mutation No
                1R0Z X-ray 2.35 Å Escherichia coli
Click to Show/Hide the Details
[ 1]
Structure
Click to Save PDB File in TXT Format
Corresponding chain A/B/C/D
Sequence Length 389-673 Mutation Yes
                1R10 X-ray 3 Å Escherichia coli
Click to Show/Hide the Details
[ 1]
Structure
Click to Save PDB File in TXT Format
Corresponding chain A/B
Sequence Length 389-673 Mutation No
                1XF9 X-ray 2.7 Å Escherichia coli
Click to Show/Hide the Details
[ 2]
Structure
Click to Save PDB File in TXT Format
Corresponding chain A/B/C/D
Sequence Length 389-670 Mutation Yes
                1XFA X-ray 3.1 Å Escherichia coli
Click to Show/Hide the Details
[ 2]
Structure
Click to Save PDB File in TXT Format
Corresponding chain A/B
Sequence Length 389-670 Mutation Yes
                3SI7 X-ray 2.25 Å Escherichia coli
Click to Show/Hide the Details
[ 3]
Structure
Click to Save PDB File in TXT Format
Corresponding chain A/B/C/D
Sequence Length 389-673 Mutation No
Rattus norvegicus (Rat)
        Gene Name Cftr
        UniProt ID
P34158
        UniProt Entry
CFTR_RAT
        3D Structure

Method:Homology modeling

Teplate PDB:5UAK_A

Sequence Length:1476

Identity:77.92%

Click to Save PDB File in TXT Format
        Performance Minimized Score -3200.166 kcal/mol
Ramachandra Favored

Medium
QMEANBrane Quality

Medium
        Ramachandran Plot

Ramz Z Score:-1.19 ±0.2

Residues in Favored Region:1427

Ramachandran favored:96.81%

Number of Outliers:11

Ramachandran outliers:0.75%
Click to Save Ramachandran Plot in PNG Format
        Local Quality

QMEANBrane Score:0.75
Click to Save Local Quality Plot in PNG Format
Oryctolagus cuniculus (Rabbit)
        Gene Name CFTR
        UniProt ID
Q00554
        UniProt Entry
CFTR_RABIT
        3D Structure

Method:Homology modeling

Teplate PDB:5UAK_A

Sequence Length:1481

Identity:92.235%

Click to Save PDB File in TXT Format
        Performance Minimized Score -3338.966 kcal/mol
Ramachandra Favored

Medium
QMEANBrane Quality

Medium
        Ramachandran Plot

Ramz Z Score:-1.26 ±0.2

Residues in Favored Region:1441

Ramachandran favored:97.43%

Number of Outliers:5

Ramachandran outliers:0.34%
Click to Save Ramachandran Plot in PNG Format
        Local Quality

QMEANBrane Score:0.75
Click to Save Local Quality Plot in PNG Format
References
1 Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator. EMBO J. 2004 Jan 28;23(2):282-93.
2 Side chain and backbone contributions of Phe508 to CFTR folding. Nat Struct Mol Biol. 2005 Jan;12(1):10-6.
3 Requirements for efficient correction of F508 CFTR revealed by analyses of evolved sequences. Cell. 2012 Jan 20;148(1-2):164-74.
4 Conformational Changes of CFTR upon Phosphorylation and ATP Binding. Cell. 2017 Jul 27;170(3):483-491.e8.
5 Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation. Biochemistry. 1999 Jun 8;38(23):7453-61.

If you find any error in data or bug in web service, please kindly report it to Dr. Li and Dr. Fu.