Structure of PDB 3d1r Chain A

Receptor sequence
>3d1rA (length=321) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MRRELAIEFSRVTESAALAGYKWLGRGDKNTADGAAVNAMRIMLNQVNID
GTIVIGEGEIAEAPMLYIGEKVGTGRGDAVDIAVDPIEGTRMTAMGQANA
LAVLAVGDKGCFLNAPDMYMEKLIVGPGAKGTIDLNLPLADNLRNVAAAL
GKPLSELTVTILAKPRHDAVIAEMQQLGVRVFAIPDGDVAASILTCMPDS
EVDVLYGIGGAPEGVVSAAVIRALDGDMNGRLLARHDVKGDNENRRIGEQ
ELARCKAMGIEAGKVLRLGDMARSDNVIFSATGITKGDLLEGISRKGNIA
TTETLLIRGKSTIRRIQSIHY
3D structure
PDB3d1r Structural and Biochemical Characterization of the Type II Fructose-1,6-bisphosphatase GlpX from Escherichia coli.
ChainA
Resolution1.85 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FBP A E88 G89 T90 Y119 K164 R166 D186 G187 D188 E213 E88 G89 T90 Y119 K164 R166 D186 G187 D188 E213
BS02 CA A D85 E88 E213 D85 E88 E213
BS03 CA A D33 E57 D33 E57
BS04 MG A L194 M197 S200 V202 L194 M197 S200 V202
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0030145 manganese ion binding
GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006071 glycerol metabolic process
GO:0006094 gluconeogenesis
GO:0030388 fructose 1,6-bisphosphate metabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3d1r, PDBe:3d1r, PDBj:3d1r
PDBsum3d1r
PubMed19073594
UniProtP0A9C9|GLPX_ECOLI Fructose-1,6-bisphosphatase 1 class 2 (Gene Name=glpX)

[Back to BioLiP]