Structure of PDB 5eqv Chain A

Receptor sequence
>5eqvA (length=336) Species: 214092 (Yersinia pestis CO92) [Search protein sequence]
AATVDLRVLETTDLHSNMMDFDYYKDKPTEKFGLVRTASLIIAARQQATN
SVLVDNGDVIQGSPLGDYIAAKGLNDGEIHPVYKAMNTLDYAVGNIGNHE
FNYGLDYLKKSLAGAKFPYVNANVIDVKTGKPLFQPYLIIDTPVKDRDGK
SHNLRIGYIGFVPPQVMIWDKANLSGKVTVNDITETAKKWVPEMREQGAD
LVVAIPHSGLSSDPYKTMAENSVYYLSQVPGIDAIMFGHAHGVFPSKDFA
AIKGADITQGTLNGIPAVMPGQWGDHLGVVDFVLNNDQGKWQVIDAKAEA
RPIYDKTAQKSLAAENAKLVEVLAVDHQSTRDFVSQ
3D structure
PDB5eqv 1.45 Angstrom Crystal Structure of Bifunctional 2',3'-cyclic Nucleotide 2'-phosphodiesterase/3'-Nucleotidase Periplasmic Precursor Protein from Yersinia pestis with Phosphate bound to the Active site.
ChainA
Resolution1.45 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) D39 H41 D84 N124 H125 N128 H233 H265 H267
Catalytic site (residue number reindexed from 1) D13 H15 D58 N98 H99 N102 H207 H239 H241
Enzyme Commision number 3.1.3.6: 3'-nucleotidase.
3.1.4.16: 2',3'-cyclic-nucleotide 2'-phosphodiesterase.
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 FE A D84 N124 H233 H265 D58 N98 H207 H239
BS02 FE A D39 H41 D84 H267 D13 H15 D58 H241
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046872 metal ion binding
Biological Process
GO:0009166 nucleotide catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5eqv, PDBe:5eqv, PDBj:5eqv
PDBsum5eqv
PubMed
UniProtA0A5P8YBY3

[Back to BioLiP]