Structure of PDB 1s2k Chain A

Receptor sequence
>1s2kA (length=199) Species: 5539 (Scytalidium lignicola) [Search protein sequence]
TVESNWGGAILIGSDFDTVSATANVPSASGGSSAAGTAWVGIDGDTCQTA
ILQTGFDWYGDGTYDAWYEWEVSITISEGDSIQMSVTATSDTSGSATLEN
LTTGQKVSKSFSNESSGSLCRTNAEFIIEDFEECNSNGSDCEFVPFASFS
PAVEFTDCSVTSDGESVSLDDAQITQVIINNQDVTDCSVSGTTVSCSYV
3D structure
PDB1s2k The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q53 E136
Catalytic site (residue number reindexed from 1) Q53 E129
Enzyme Commision number 3.4.23.32: scytalidopepsin B.
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 Q53 D57 W67 E136 F138 E139 E140 Q53 D57 W67 E129 F131 E132 E133
BS02 TYR A N5 W6 N5 W6
Gene Ontology
Molecular Function
GO:0070007 glutamic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1s2k, PDBe:1s2k, PDBj:1s2k
PDBsum1s2k
PubMed14993599
UniProtP15369|PRTB_SCYLI Scytalidopepsin B

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