Structure of PDB 5a67 Chain A

Receptor sequence
>5a67A (length=206) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
GAMEVEVKLRLLTAAAHLRLTTLLTPYHLKTLHQRNTFFDTPKNDLSLRR
AVLRLRFLQNAPSPPRCIVSLKAKPTLANGISRVEEDEEEIEYWIGKECV
ESPAKLSDIGSRVLKRVKEEYGFNDFLGFVCLGGFENVRNVYEWRGVKLE
VDETKYDFGNCYEIECETEEPERVKTMIEEFLTEEKIEFSNSDMTKFAVF
RSGKLP
3D structure
PDB5a67 Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.
ChainA
Resolution1.3 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 3.6.1.-
3.6.1.25: triphosphatase.
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 MN A E4 E169 E6 E165
BS02 3PO A E4 K6 R52 R54 K76 R143 E169 T199 K200 E6 K8 R54 R56 K72 R139 E165 T195 K196
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016462 pyrophosphatase activity
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0050355 inorganic triphosphate phosphatase activity
Biological Process
GO:0048364 root development
Cellular Component
GO:0005634 nucleus
GO:0005680 anaphase-promoting complex
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:5a67, PDBe:5a67, PDBj:5a67
PDBsum5a67
PubMed26221030
UniProtQ9SIY3|TTM3_ARATH Triphosphate tunnel metalloenzyme 3 (Gene Name=TTM3)

[Back to BioLiP]