Structure of PDB 4pv2 Chain A

Receptor sequence
>4pv2A (length=155) Species: 3885 (Phaseolus vulgaris) [Search protein sequence]
GGWAIAVHGGAGVDPTLPLERQEEAKQLLTRCLNLGISALNSNVPAIDVV
ELVVRELETDPLFNSGRGSALTEKGTVEMEASIMDGPKRRCGAVSGLTTV
KNPISLARLVMDKSPHSYIAFSGAEDFARQQGVEVVDNEYFVTPDNVGML
KLAKE
3D structure
PDB4pv2 Na+/K+ exchange switches the catalytic apparatus of potassium-dependent plant L-asparaginase
ChainA
Resolution1.79 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) S66
Catalytic site (residue number reindexed from 1) S65
Enzyme Commision number 3.5.1.1: asparaginase.
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 NA A L58 E59 T60 D61 P62 S66 G67 R68 L57 E58 T59 D60 P61 S65 G66 R67
BS02 NA A V111 M112 S115 H117 V110 M111 S114 H116
BS03 K A L58 E59 D61 P62 L63 F64 N65 S66 R68 L57 E58 D60 P61 L62 F63 N64 S65 R67
BS04 K A C92 V111 M112 S115 P116 H117 S118 C91 V110 M111 S114 P115 H116 S117
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:4pv2, PDBe:4pv2, PDBj:4pv2
PDBsum4pv2
PubMed25004963
UniProtV7CU13

[Back to BioLiP]