Structure of PDB 3jyf Chain A

Receptor sequence
>3jyfA (length=336) Species: 272620 (Klebsiella pneumoniae subsp. pneumoniae MGH 78578) [Search protein sequence]
AATVDLRIMETTDLHSNMMDFDYYKDAATEKFGLVRTASLIEQARAEVKN
SVLVDNGDVIQGSPLGDYMAAKGLKEGDVHPVYKAMNTLNYAVGNLGNHE
FNYGLDFLHKALAGAKFPYVNANIIDAKTGKPMFTPYLIQDTRVVDSDGQ
IHTLRIGYIGFVPPQIMTWDKANLNGKVTVNDITETARKYIPEMRAKGAD
VVVVVAHSGLSADPYQAMAENSVYYLSQVPGVDAIMFGHAHAVFPGKDFA
NIKGADIAKGTLNGVPAVMPGMWGDHLGVVDLVLNNDSGKWQVTQSKAEA
RPIYDAVAKKSLAAEDGKLVSVLKADHDATREFVSK
3D structure
PDB3jyf The crystal structure of a 2,3-cyclic nucleotide 2-phosphodiesterase/3-nucleotidase bifunctional periplasmic precursor protein from Klebsiella pneumoniae subsp. pneumoniae MGH 78578
ChainA
Resolution2.43 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D16 H18 D61 N101 H102 N105 H210 H242 H244
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 MN A D16 H18 D61 H244 D13 H15 D58 H241
BS02 MN A D61 N101 H210 H242 D58 N98 H207 H239
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3jyf, PDBe:3jyf, PDBj:3jyf
PDBsum3jyf
PubMed
UniProtA6THC4

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