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PDBsum entry 3ix1
Go to PDB code:
Biosynthetic protein
PDB id
3ix1
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Contents
Protein chains
301 a.a.
*
Ligands
NFM
×2
Waters
×259
*
Residue conservation analysis
PDB id:
3ix1
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Biosynthetic protein
Title:
Periplasmic n-formyl-4-amino-5-aminomethyl-2-methylpyrimidine binding protein from bacillus halodurans
Structure:
N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine binding protein. Chain: a, b. Synonym: thiamine biosynthesis protein. Engineered: yes
Source:
Bacillus halodurans c-125. Organism_taxid: 272558. Strain: c-125 / dsm 18197 / ferm 7344 / jcm 9153. Atcc: baa-125. Gene: bh2682. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.40Å
R-factor:
0.203
R-free:
0.264
Authors:
S.Bale,K.R.Rajashankar,K.Perry,T.P.Begley,S.E.Ealick
Key ref:
S.Bale et al. (2010). HMP binding protein ThiY and HMP-P synthase THI5 are structural homologues.
Biochemistry
,
49
, 8929-8936.
PubMed id:
20873853
Date:
03-Sep-09
Release date:
13-Oct-10
PROCHECK
Headers
References
Protein chains
?
Q9K9G5
(THIY_BACHD) - Formylaminopyrimidine-binding protein from Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Seq:
Struc:
330 a.a.
301 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
E.C.?
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Biochemistry
49
:8929-8936 (2010)
PubMed id:
20873853
HMP binding protein ThiY and HMP-P synthase THI5 are structural homologues.
S.Bale,
K.R.Rajashankar,
K.Perry,
T.P.Begley,
S.E.Ealick.
ABSTRACT
No abstract given.
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