Structure of PDB 3rva Chain A

Receptor sequence
>3rvaA (length=445) Species: 28108 (Alteromonas macleodii) [Search protein sequence]
SQHKATYQQHIEELQARTREALQREGLDGLVIHSGQGKRLFLDDNHYPFK
VNPQFKAWVPVIDNPNCWLVVNGVDKPTLIFYRPEDFWHKVPPEPNDFWT
DSFDIKLLQQADAVEKFLPYDKSRFAYVGEYIEVAKALGFDNVNPDRVLH
YLHYQRAYKTDYELDCMREANKLAVAGHKAAEQAFREGKSEFDINLAYAA
ASRQGDNDVPYTSIVALNEHASILHYMQCDTVAPKESRSFLIDAGANYHG
YAADITRTYAQEGVHNSAMFRDLIQAVDKVTLTLVDSLKPGVAYTDIHLL
AHDGIAQILHDTGMVNLTPPEIVEMGITRTFFPHGIGHFLGLQVHDVGGL
VNDDRGTPKPAPDDHPFLRCTRMVEARQVFTIEPGLYFIDSLLRDLKATP
ASKYINWDTIDAYKPFGGIRIEDNIIVHRDKNENMTRDLDLNLEH
3D structure
PDB3rva Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D45 H226 D244 D255 H335 H339 H346 E384 Y388 R421 E423
Catalytic site (residue number reindexed from 1) D44 H225 D243 D254 H334 H338 H345 E383 Y387 R420 E422
Enzyme Commision number 3.4.13.9: Xaa-Pro dipeptidase.
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 D244 D255 E423 D243 D254 E422
BS02 MN A D255 H339 T382 E384 E423 D254 H338 T381 E383 E422
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008235 metalloexopeptidase activity
GO:0008237 metallopeptidase activity
GO:0016795 phosphoric triester hydrolase activity
GO:0016805 dipeptidase activity
GO:0046872 metal ion binding
GO:0102009 proline dipeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:3rva, PDBe:3rva, PDBj:3rva
PDBsum3rva
PubMed23545636
UniProtF8UVJ4

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