 |
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Transferase
|
 |
|
Title:
|
 |
Human phosphatidylinositol-4-phosphate 5-kinase, type ii, gamma
|
|
Structure:
|
 |
Phosphatidylinositol-4-phosphate 5-kinase, type ii, gamma. Chain: a, b, c, d. Engineered: yes
|
|
Source:
|
 |
Homo sapiens. Human. Organism_taxid: 9606. Gene: pip5k2c. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
Biol. unit:
|
 |
Tetramer (from
)
|
|
Resolution:
|
 |
|
2.80Å
|
R-factor:
|
0.261
|
R-free:
|
0.297
|
|
|
Authors:
|
 |
J.Uppenberg,M.Hogbom,D.Ogg,C.Arrowsmith,H.Berglund, R.Collins,M.Ehn,S.Flodin,A.Flores,S.Graslund,L.Holmberg- Schiavone,A.Edwards,M.Hammarstrom,T.Kotenyova,P.Nilsson- Ehle,P.Nordlund,T.Nyman,C.Persson,J.Sagemark,P.Stenmark, M.Sundstrom,A.G.Thorsell,S.Van Den Berg,J.Weigelt, B.M.Hallberg,Structural Genomics Consortium (Sgc)
|
|
Key ref:
|
 |
A.G.Thorsell
et al.
Structure of human phosphatidylinositol-4-Phosphate 5-Kinase, Type ii, Gamma.
To be published,
|
 |
|
Date:
|
 |
|
31-Mar-06
|
Release date:
|
02-May-06
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
|
 |
|
|
 |
 |
 |
 |
Enzyme class:
|
 |
Chains A, B, C, D:
E.C.2.7.1.149
- 1-phosphatidylinositol-5-phosphate 4-kinase.
|
|
 |
 |
 |
 |
 |

Pathway:
|
 |
1-Phosphatidyl-myo-inositol Metabolism
|
 |
 |
 |
 |
 |
Reaction:
|
 |
ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl- 1D-myo-inositol 4,5-bisphosphate
|
 |
 |
 |
 |
 |
ATP
|
+
|
1-phosphatidyl-1D-myo-inositol 5-phosphate
|
=
|
ADP
|
+
|
1-phosphatidyl- 1D-myo-inositol 4,5-bisphosphate
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
 |
 |
|
 |
|
 |
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
 |
 |
 |
|
 |
 |
 |
 |
|
 |
|
Cellular component
|
membrane
|
2 terms
|
 |
|
Biological process
|
phosphatidylinositol metabolic process
|
1 term
|
 |
|
Biochemical function
|
nucleotide binding
|
7 terms
|
 |
|
|
 |
 |
 |
 |
 |
 |
| |