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
Go to PDB code:
Transferase
PDB id
1vqv
Contents
Protein chains
292 a.a.
*
Ligands
PO4
×4
Waters
×116
*
Residue conservation analysis
PDB id:
1vqv
Links
PDBe
RCSB
SRS
MMDB
JenaLib
OCA
PDBWiki
Proteopedia
CATH
SCOP
FSSP
HSSP
PDBSWS
PQS
ProSAT
EDS
Whatcheck
Name:
Transferase
Title:
Crystal structure of thiamine monophosphate kinase (thil) from aquifex aeolicus
Structure:
Thiamine monophosphate kinase. Chain: a, b. Engineered: yes
Source:
Aquifex aeolicus. Organism_taxid: 63363. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit:
Dimer (from
PQS
)
Resolution:
2.65Å
R-factor:
0.238
R-free:
0.260
Authors:
S.Eswaramoorthy,S.Swaminathan,S.K.Burley,New York Sgx Research Center For Structural Genomics (Nysgxrc)
Key ref:
S.Eswaramoorthy and s.swaminathan Crystal structure of thiamine monophosphate kinase (thil) from aquifex aeolicus.
To be published
,
Date:
05-Jan-05
Release date:
11-Jan-05
Supersedes:
1yaw
PROCHECK
Headers
References
Protein chains
?
O67883
(O67883_AQUAE) - Thiamine monophosphate kinase
Seq:
Struc:
306 a.a.
292 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
E.C.2.7.4.16
- Thiamine-phosphate kinase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
ATP + thiamine phosphate = ADP + thiamine diphosphate
ATP
+
thiamine phosphate
=
ADP
+
thiamine diphosphate
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
Gene Ontology (GO) functional annotation
Biological process
phosphorylation
2 terms
Biochemical function
catalytic activity
6 terms