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 3suz
Go to PDB code:
Protein binding
PDB id
3suz
Loading ...
Contents
Protein chain
287 a.a.
Waters
×51
PDB id:
3suz
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Protein binding
Title:
Crystal structure of rat mint2 ppc
Structure:
Amyloid beta a4 precursor protein-binding family a member 2. Chain: a. Fragment: residues 365-750. Synonym: adapter protein x11beta, neuron-specific x11l protein, neuronal munc18-1-interacting protein 2, mint-2. Engineered: yes
Source:
Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: mint2. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.70Å
R-factor:
0.265
R-free:
0.289
Authors:
Y.Shen,J.Long,X.Yan,X.Xie
Key ref:
X.Xie et al. (2013). Open-closed motion of Mint2 regulates APP metabolism.
J Mol Cell Biol
,
5
, 48-56.
PubMed id:
22730553
DOI:
10.1093/jmcb/mjs033
Date:
11-Jul-11
Release date:
11-Jul-12
PROCHECK
Headers
References
Protein chain
?
O35431
(APBA2_RAT) - Amyloid-beta A4 precursor protein-binding family A member 2 from Rattus norvegicus
Seq:
Struc:
 
Seq:
Struc:
750 a.a.
287 a.a.
*
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 8 residue positions (black crosses)
Enzyme reactions
Enzyme class:
E.C.?
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
DOI no:
10.1093/jmcb/mjs033
J Mol Cell Biol
5
:48-56 (2013)
PubMed id:
22730553
Open-closed motion of Mint2 regulates APP metabolism.
X.Xie,
X.Yan,
Z.Wang,
H.Zhou,
W.Diao,
W.Zhou,
J.Long,
Y.Shen.
ABSTRACT
No abstract given.
'); } }