Structure of PDB 1bhn Chain E

Receptor sequence
>1bhnE (length=151) Species: 9913 (Bos taurus) [Search protein sequence]
ANSERTFIAIKPDGVQRGLIGEIIKRFEQKGFRLVAMKFMRASEDLLKEH
YIDLKDRPFFAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKP
GTIRGDFCIQVGRNIIHGSDSVESAEKEIALWFHPEELVNYKSCAQNWIY
E
3D structure
PDB1bhn The three-dimensional structures of two isoforms of nucleoside diphosphate kinase from bovine retina.
ChainE
Resolution2.4 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) K12 Y52 N115 H118 E129
Catalytic site (residue number reindexed from 1) K11 Y51 N114 H117 E128
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 35G E K12 F60 N115 H118 K11 F59 N114 H117
BS02 GDP E F60 R88 T94 V112 N115 F59 R87 T93 V111 N114
Gene Ontology
Molecular Function
GO:0004550 nucleoside diphosphate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0006183 GTP biosynthetic process
GO:0006228 UTP biosynthetic process
GO:0006241 CTP biosynthetic process
GO:0006897 endocytosis
GO:0007399 nervous system development
GO:0009117 nucleotide metabolic process
GO:0016310 phosphorylation
GO:0030154 cell differentiation
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005886 plasma membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1bhn, PDBe:1bhn, PDBj:1bhn
PDBsum1bhn
PubMed10329774
UniProtP52174|NDKA1_BOVIN Nucleoside diphosphate kinase A 1 (Gene Name=NME1-1)

[Back to BioLiP]