Structure of PDB 5nrz Chain A

Receptor sequence
>5nrzA (length=381) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence]
SPIEEQATRLLKEVPLIDGHNDFPYMIRGWFRNDINGQDAHLYDMPIGQT
DLQRLQKGLLGGQFWSAFVPCPKNPDKEVGSLEALRQTLQQLDVIHRLIE
RHPTILQFADSAASIWSSFRAGRVASLIGIEGLHQIADSVSALRMLHRLG
VRYVTLTHNCHNAFADAATVSPELHGGLSRKGERLIRELNRMGMMIDLSH
TSHEAQTQALRLSRAPVIYSHSSIYSLRAHARNVTDENLHLLHRNRGVVM
ICFLRELLASEADQATLAHVIDHIIYAGTRIGYEHVGIGSDFDGMLRGPD
GLHDVSCYPALVAGLLERGVSEEDVKRVMGLNVIRVLEEVERVAAELQGA
GEECLCDELDEVWNEDIKEQLTRERERVRKL
3D structure
PDB5nrz Gliotoxin Biosynthesis: Structure, Mechanism, and Metal Promiscuity of Carboxypeptidase GliJ.
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H23 D25 E134 H161 H203 H224 D294
Catalytic site (residue number reindexed from 1) H20 D22 E131 H158 H200 H221 D291
Enzyme Commision number 3.4.13.19: membrane 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 E134 H203 H224 E131 H200 H221
BS02 MN A H23 D25 E134 H20 D22 E131
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0016805 dipeptidase activity
GO:0046872 metal ion binding
GO:0070573 metallodipeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0043386 mycotoxin biosynthetic process
GO:0052562 symbiont-mediated suppression of host immune response
GO:2001310 gliotoxin biosynthetic process
Cellular Component
GO:0005575 cellular_component

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5nrz, PDBe:5nrz, PDBj:5nrz
PDBsum5nrz
PubMed28525266
UniProtQ4WMJ8|GLIJ_ASPFU Dipeptidase gliJ (Gene Name=gliJ)

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