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PDBsum entry 4g8a

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protein ligands Protein-protein interface(s) links
Immune system PDB id
4g8a

 

 

 

 

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Contents
Protein chains
601 a.a.
140 a.a.
Ligands
NAG-NAG ×4
NAG ×4
LP4-LP5-DAO-MYR-
KDO
×2
Waters ×39
PDB id:
4g8a
Name: Immune system
Title: Crystal structure of human tlr4 polymorphic variant d299g and t399i in complex with md-2 and lps
Structure: Toll-like receptor 4. Chain: a, b. Fragment: unp residues 23-629. Synonym: htoll, protein tlr4. Engineered: yes. Mutation: yes. Lymphocyte antigen 96. Chain: c, d. Synonym: ly-96, esop-1, protein md-2.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: tlr4. Expressed in: drosophila. Expression_system_taxid: 7215. Expression_system_cell_line: s2. Gene: ly96, esop1, md2.
Resolution:
2.40Å     R-factor:   0.202     R-free:   0.249
Authors: U.Ohto,T.Shimizu
Key ref: U.Ohto et al. (2012). Structural analyses of human Toll-like receptor 4 polymorphisms D299G and T399I. J Biol Chem, 287, 40611-40617. PubMed id: 23055527
Date:
23-Jul-12     Release date:   17-Oct-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O00206  (TLR4_HUMAN) -  Toll-like receptor 4 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
839 a.a.
601 a.a.*
Protein chains
Pfam   ArchSchema ?
Q9Y6Y9  (LY96_HUMAN) -  Lymphocyte antigen 96 from Homo sapiens
Seq:
Struc:
160 a.a.
140 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.3.2.2.6  - ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: NAD+ + H2O = ADP-D-ribose + nicotinamide + H+
NAD(+)
+ H2O
= ADP-D-ribose
+ nicotinamide
+ H(+)
Bound ligand (Het Group name = NAG)
matches with 43.75% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Biol Chem 287:40611-40617 (2012)
PubMed id: 23055527  
 
 
Structural analyses of human Toll-like receptor 4 polymorphisms D299G and T399I.
U.Ohto, N.Yamakawa, S.Akashi-Takamura, K.Miyake, T.Shimizu.
 
  ABSTRACT  
 
No abstract given.

 

 

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