Structure of PDB 6bve Chain A

Receptor sequence
>6bveA (length=242) Species: 1111708 (Synechocystis sp. PCC 6803 substr. Kazusa) [Search protein sequence]
MRKIIIAGNWKMHKTQAEAQAFLQGFKPLIEDAAESREVVLCVPFTDLSG
MSQQLHGGRVRLGAQNVHWEASGAYTGEISAAMLTEIGIHYVVIGHSERR
QYFGETDETANLRVLAAQKAGLIPILCVGESKAQRDAGETEQVIVDQVKK
GLVNVDQSNLVIAYEPIWAIGTGDTCAATEANRVIGLIREQLTNSQVTIQ
YGGSVNANNVDEIMAQPEIDGALVGGASLEPQSFARIVNFQP
3D structure
PDB6bve Structural Basis for the Limited Response to Oxidative and Thiol-Conjugating Agents by Triosephosphate Isomerase From the Photosynthetic BacteriaSynechocystis.
ChainA
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) N9 K11 H96 E98 E165 G171 S204
Catalytic site (residue number reindexed from 1) N9 K11 H96 E98 E165 G171 S204
Enzyme Commision number 5.3.1.1: triose-phosphate isomerase.
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 PGA A K11 H96 E165 I170 G171 G203 S204 G225 G226 K11 H96 E165 I170 G171 G203 S204 G225 G226
Gene Ontology
Molecular Function
GO:0004807 triose-phosphate isomerase activity
GO:0016853 isomerase activity
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0019563 glycerol catabolic process
GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6bve, PDBe:6bve, PDBj:6bve
PDBsum6bve
PubMed30538993
UniProtQ59994|TPIS_SYNY3 Triosephosphate isomerase (Gene Name=tpiA)

[Back to BioLiP]