Structure of PDB 3ngt Chain N

Receptor sequence
>3ngtN (length=150) Species: 5664 (Leishmania major) [Search protein sequence]
SSERTFIAVKPDGVQRGLVGEIIARFERKGYKLVALKILQPTTEQAQGHY
KDLCSKPFFPALVKYFSSGPIVCMVWEGKNVVKSGRVLLGATNPADSQPG
TIRGDFAVDVGRNVCHGSDSVESAEREIAFWFKADEIASWTSHSVSQIYE
3D structure
PDB3ngt Molecular adaptability of nucleoside diphosphate kinase b from trypanosomatid parasites: stability, oligomerization and structural determinants of nucleotide binding.
ChainN
Resolution2.57 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) K11 Y51 N114 H117 E128
Catalytic site (residue number reindexed from 1) K10 Y50 N113 H116 E127
Enzyme Commision number 2.7.4.6: nucleoside-diphosphate kinase.
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 AMP N K11 Y51 L54 F59 T93 V111 N114 H117 K10 Y50 L53 F58 T92 V110 N113 H116
Gene Ontology
Molecular Function
GO:0004550 nucleoside diphosphate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0006183 GTP biosynthetic process
GO:0006228 UTP biosynthetic process
GO:0006241 CTP biosynthetic process
GO:0009142 nucleoside triphosphate biosynthetic process
GO:0016310 phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0097014 ciliary plasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3ngt, PDBe:3ngt, PDBj:3ngt
PDBsum3ngt
PubMed21528129
UniProtQ9U1E1

[Back to BioLiP]