Structure of PDB 3ive Chain A

Receptor sequence
>3iveA (length=495) Species: 217992 (Escherichia coli O6) [Search protein sequence]
AKDVTIIYTNDLHAHVEPYKVPWIADGKRDIGGWANITTLVKQEKAKNKA
TWFFDAGDYFTGPYISSLTKGKAIIDIMNTMPFDAVTIGNHEFDHGWDNT
LLQLSQAKFPIVQGNIFYQNSSKSFWDKPYTIIEKDGVKIGVIGLHGVFA
FNDTVSAATRVGIEARDEIKWLQRYIDELKGKVDLTVALIHEGVPARQSS
MDVRRALDKDIQTASQVKGLDILITGHAHVGTPEPIKVGNTLILSTDSGG
IDVGKLVLDYKEKPHNFTVKNFELKTIYADEWKPDQQTKQVIDGWNKKLD
EVVQQTVAQSPVELKRAYGESASLGNLAADALLAAAGKNTQLALTNSGGI
RNEIPAGAITMGGVISTFPFPNELVTMELTGKQLRSLMEHGASLSNGVLQ
VSKGLEMKYDSSKPVGQRVITLTLNGKPIEDATVYHIATQSFLADGGDGF
TAFTEGKARNITGGYYVYHAVVDYFKAGNTITDEQLNGMRVKDIK
3D structure
PDB3ive Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Cytidine
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D32 H34 D79 N111 H112 D115 H212 H251 H253 Y342 R375
Catalytic site (residue number reindexed from 1) D11 H13 D58 N90 H91 D94 H191 H227 H229 Y318 R351
Enzyme Commision number ?
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 D32 H34 D79 H253 D11 H13 D58 H229
BS02 FE A D79 N111 H212 H251 D58 N90 H191 H227
BS03 CTN A H112 T175 N370 G372 R375 F394 N396 F466 D472 H91 T154 N346 G348 R351 F370 N372 F442 D448
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:3ive, PDBe:3ive, PDBj:3ive
PDBsum3ive
PubMed
UniProtA0A0H2VD83

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