Structure of PDB 5b62 Chain A Binding Site BS01

Receptor Information

>5b62 Chain A (length=426) Species: 889517 (Saccharomyces cerevisiae CEN.PK113-7D) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

TKLLVSLKVLVIQLNPQIGQVDQTIKRTWSILDKVTKSATYVKPDIILFP
EFALTGYSFHARKDILPYVTKKDEGPSFELAKSISEKFQCYTIIGYPEED
DEQKLYNSALVVNPQGGQIFNYRKTFLYDTEMNWDCEENPEGFQTFPMDF
SKCAKLSNEDSYNRDVTLKASIGISMDLSPYKFMAPFNHFEFSSFCVDNN
VELILCPMAWLNSTSITDKQTLHNNSLLEAAKNKIAFALKEQGLPLAGSQ
GIYQLKIGDSQRTPRVPSDDSTSEYKDMDEPDMSNVNYWILRFFPFLYFK
LRINWFKNSSLIESILGKTRMPLDHEYYKDLLDSEEVIKDTVLEKTFLGT
SLGQPWKFQGKNAILVLANRCGTEDGTTIFAGSSGIYKFNGKKSLDSLNE
SVELLGNLGKGLEGAILREVQFEVFR

Ligand information

>5b62 Chain B (length=3) Species: 889517 (Saccharomyces cerevisiae CEN.PK113-7D) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

NEA

Receptor-Ligand Complex Structure

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Structure summary

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PDB	5b62 Structural basis for dual specificity of yeast N-terminal amidase in the N-end rule pathway.
Resolution	3.042 Å
Binding residue (original residue number in PDB)	Y69 Y140 S187 M188 W222 L223 T229 Y300
Binding residue (residue number reindexed from 1)	Y57 Y128 S175 M176 W210 L211 T217 Y288

Enzymatic activity

Enzyme Commision number

Gene Ontology

	Molecular Function
GO:0008418	protein-N-terminal asparagine amidohydrolase activity
GO:0070773	protein-N-terminal glutamine amidohydrolase activity

	Biological Process
GO:0030163	protein catabolic process

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Molecular Function

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Biological Process

External links

PDB	RCSB:5b62, PDBe:5b62, PDBj:5b62
PDBsum	5b62
PubMed	27791147
UniProt	N1P8Q8

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