Structure of PDB 1ize Chain A

Receptor sequence
>1izeA (length=323) Species: 5062 (Aspergillus oryzae) [Search protein sequence]
AATGSVTTNPTSNDEEYITQVTVGDDTLGLDFDTGSADLWVFSSQTPSSE
RSGHDYYTPGSSAQKIDGATWSISYGDGSSASGDVYKDKVTVGGVSYDSQ
AVESAEKVSSEFTQDTANDGLLGLAFSSINTVQPTPQKTFFDNVKSSLSE
PIFAVALKHNAPGVYDFGYTDSSKYTGSITYTDVDNSQGFWGFTADGYSI
GSDSSSDSITGIADTGTTLLLLDDSIVDAYYEQVNGASYDSSQGGYVFPS
SASLPDFSVTIGDYTATVPGEYISFADVGNGQTFGGIQSNSGIGFSIFGD
VFLKSQYVVFDASGPRLGFAAQA
3D structure
PDB1ize Crystal structures of Aspergillus oryzae aspartic proteinase and its complex with an inhibitor pepstatin at 1.9A resolution.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D33 S36 D38 W40 Y75 D214 T217
Catalytic site (residue number reindexed from 1) D33 S36 D38 W40 Y75 D214 T217
Enzyme Commision number 3.4.23.18: aspergillopepsin I.
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 peptide A E15 D33 G35 S74 Y75 G76 D77 E111 F190 D214 G216 T217 T218 E15 D33 G35 S74 Y75 G76 D77 E111 F190 D214 G216 T217 T218
BS02 MAN A T3 Y169 T3 Y169
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1ize, PDBe:1ize, PDBj:1ize
PDBsum1ize
PubMed12595261
UniProtP0CU33|PEPA_ASPOZ Aspergillopepsin-1 (Gene Name=pepA)

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