Structure of PDB 5xgw Chain B

Receptor sequence
>5xgwB (length=374) Species: 167879 (Colwellia psychrerythraea 34H) [Search protein sequence]
TMLILLCNVNIYAPNPLGIKDVLIAGNKIAAIYDHGQGEITIPKQWPVKV
INFDGAILTPGFIDSHAHITGGGGEAGFATQVPPVGLTEFTHAGVTTVVG
LLGTDDTTRSTENLLSRVYGLREEGLSAYCWTGGYHFPLTTITGSAKSDI
AFLEPVIGIGEFAISDHRSSQPTFEEVIRLASETHVAGLITGKAGVIHFH
LGDGERRLELIERAIRETELPARVFNPTHVNRNKPLFEDSCKLLSKGCHI
DLTAFPAGTAQPGWEACDAIEMAVERQLPLEQITLSSDGGGGRASTLGET
LVATLNKGLSLETVLPMLTSNVANILRFKNKGQIAVGFDADLLVMNEKYE
ITDVMAQGVWHKQNNQTMIKGTFE
3D structure
PDB5xgw Crystal structure and functional characterization of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea strain 34H.
ChainB
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H71 H73 E166 H205 H234 D293
Catalytic site (residue number reindexed from 1) H66 H68 E161 H200 H229 D288
Enzyme Commision number 3.4.19.-
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 ZN B H71 H73 E166 D293 H66 H68 E161 D288
BS02 ZN B E166 H205 H234 E161 H200 H229
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0008798 beta-aspartyl-peptidase activity
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5xgw, PDBe:5xgw, PDBj:5xgw
PDBsum5xgw
PubMed28723955
UniProtQ484B6

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