Structure of PDB 1hpu Chain A

Receptor sequence
>1hpuA (length=525) Species: 562 (Escherichia coli) [Search protein sequence]
YEQDKTYKITVLHTNDHHGHFWRNEYGEYGLAAQKTLVDGIRKEVAAEGG
SVLLLSGGDINTGVPESDLQDAEPDFRGMNLVGYDAMAIGNHEFDNPLTV
LRQQEKWAKFPLLSANIYQKSTGERLFKPWALFKRQDLKIAVIGLTTDDT
AKIGNPEYFTDIEFRKPADEAKLVIQELQQTEKPDIIIAATHMGHYDNGE
HGSNAPGDVEMARALPAGSLAMIVGGHSQDPVCMAAENKKQVDYVPGTPC
KPDQQNGIWIVQAHEWGKYVGRADFEFRNGEMKMVNYQLIPVNLKKKVTW
EDGKSERVLYTPEIAENQQMISLLSPFQNKGKAQLEVKIGETNGRLEGDR
DKVRFVQTNMGRLILAAQMDRTGADFAVMSGGGIRDSIEAGDISYKNVLK
VQPFGNVVVYADMTGKEVIDYLTAVAQMKPDSGAYPQFANVSFVAKDGKL
NDLKIKGEPVDPAKTYRMATLNFNATGGDGYPRLDNKPGYVNTGFIDAEV
LKAYIQKSSPLDVSVYEPKGEVSWQ
3D structure
PDB1hpu Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures.
ChainA
Resolution1.85 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) D41 H43 D84 N116 H117 D120 H217 H252 Q254 R375 R379 R410
Catalytic site (residue number reindexed from 1) D16 H18 D59 N91 H92 D95 H192 H227 Q229 R350 R354 R385
Enzyme Commision number 3.1.3.5: 5'-nucleotidase.
3.6.1.45: UDP-sugar diphosphatase.
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 D84 N116 H217 H252 D59 N91 H192 H227
BS02 MN A D41 H43 D84 Q254 D16 H18 D59 Q229
BS03 A12 A N116 H117 I178 H252 R375 R379 G407 R410 F429 N431 G458 F498 D504 N91 H92 I153 H227 R350 R354 G382 R385 F404 N406 G433 F473 D479
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008252 nucleotidase activity
GO:0008253 5'-nucleotidase activity
GO:0008768 UDP-sugar diphosphatase activity
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046872 metal ion binding
GO:0106411 XMP 5'-nucleosidase activity
Biological Process
GO:0009166 nucleotide catabolic process
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1hpu, PDBe:1hpu, PDBj:1hpu
PDBsum1hpu
PubMed11491293
UniProtP07024|USHA_ECOLI Protein UshA (Gene Name=ushA)

[Back to BioLiP]