Structure of PDB 2id4 Chain B

Receptor sequence
>2id4B (length=479) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
LPVKEAEDKLSINDPLFERQWHLVNPSFPGSDINVLDLWYNNITGAGVVA
AIVDDGLDYENEDLKDNFCAEGSWDFNDNTNLPKPRLSDDYHGTRCAGEI
AAKKGNNFCGVGVGYNAKISGIRILSGDITTEDEAASLIYGLDVNDIYSC
SWGPADDGRHLQGPSDLVKKALVKGVTEGRDSKGAIYVFASGNGGTRGDN
CNYDGYTNSIYSITIGAIDHKDLHPPYSEGCSAVMAVTYSSGSGEYIHSS
DINGRCSNSHGGTSAAAPLAAGVYTLLLEANPNLTWRDVQYLSILSAVGL
EKNADGDWRDSAMGKKYSHRYGFGKIDAHKLIEMSKTWENVNAQTWFYLP
TLYVSQSTNSTEETLESVITISEKSLQDANFKRIEHVTVTVDIDTEIRGT
TTVDLISPAGIISNLGVVRPRDVSSEGFKDWTFMSVAHWGENGVGDWKIK
VKTTENGHRIDFHSWRLKLFGESIDSSKT
3D structure
PDB2id4 Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2.
ChainB
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) D175 H213 N314 S385
Catalytic site (residue number reindexed from 1) D54 H92 N193 S264
Enzyme Commision number 3.4.21.61: kexin.
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 B D176 H213 L246 I250 E255 S272 W273 G274 P275 D277 N314 S385 D55 H92 L125 I129 E134 S151 W152 G153 P154 D156 N193 S264
BS02 CA B D277 D320 E350 D156 D199 E229
BS03 CA B D135 D184 K224 N227 F229 G231 D14 D63 K103 N106 F108 G110
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2id4, PDBe:2id4, PDBj:2id4
PDBsum2id4
PubMed17426142
UniProtP13134|KEX2_YEAST Kexin (Gene Name=KEX2)

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