Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 4m4x
Go to PDB code:
Transcription
PDB id
4m4x
Loading ...
Contents
Protein chains
126 a.a.
111 a.a.
Waters
×39
PDB id:
4m4x
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Transcription
Title:
Structure and dimerization properties of the aryl hydrocarbon receptor (ahr) pas-a domain
Structure:
Aryl hydrocarbon receptor. Chain: a, b. Fragment: pas-a domain, unp residues 110-267. Synonym: ah receptor, ahr. Engineered: yes
Source:
Mus musculus. Mouse. Organism_taxid: 10090. Strain: c57bl. Gene: ahr. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.55Å
R-factor:
0.202
R-free:
0.245
Authors:
D.Wu,N.Potluri,Y.Kim,F.Rastinejad
Key ref:
D.Wu et al. (2013). Structure and dimerization properties of the aryl hydrocarbon receptor PAS-A domain.
Mol Cell Biol
,
33
, 4346-4356.
PubMed id:
24001774
DOI:
10.1128/MCB.00698-13
Date:
07-Aug-13
Release date:
18-Sep-13
PROCHECK
Headers
References
Protein chain
?
P30561
(AHR_MOUSE) - Aryl hydrocarbon receptor from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
848 a.a.
126 a.a.
*
Protein chain
?
P30561
(AHR_MOUSE) - Aryl hydrocarbon receptor from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
848 a.a.
111 a.a.
*
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 5 residue positions (black crosses)
Enzyme reactions
Enzyme class:
Chains A, B:
E.C.?
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
DOI no:
10.1128/MCB.00698-13
Mol Cell Biol
33
:4346-4356 (2013)
PubMed id:
24001774
Structure and dimerization properties of the aryl hydrocarbon receptor PAS-A domain.
D.Wu,
N.Potluri,
Y.Kim,
F.Rastinejad.
ABSTRACT
No abstract given.
'); } }