Structure of PDB 1r64 Chain A

Receptor sequence

>1r64A (length=481) Species: 4932 (Saccharomyces cerevisiae)

LLPVKEAEDKLSINDPLFERQWHLVNPSFPGSDINVLDLWYNNITGAGVV
AAIVDDGLDYENEDLKDNFCAEGSWDFNDNTNLPKPRLSDDYHGTRCAGE
IAAKKGNNFCGVGVGYNAKISGIRILSGDITTEDEAASLIYGLDVNDIYS
CSWGPADDGRHLQGPSDLVKKALVKGVTEGRDSKGAIYVFASGNGGTRGD
NCNYDGYTNSIYSITIGAIDHKDLHPPYSEGCSAVMAVTYSSGSGEYIHS
SDINGRCSNSHGGTSAAAPLAAGVYTLLLEANPNLTWRDVQYLSILSAVG
LEKNADGDWRDSAMGKKYSHRYGFGKIDAHKLIEMSKTWENVNAQTWFYL
PTLYVSQSTNSTEETLESVITISEKSLQDANFKRIEHVTVTVDIDTEIRG
TTTVDLISPAGIISNLGVVRPRDVSSEGFKDWTFMSVAHWGENGVGDWKI
KVKTTENGHRIDFHSWRLKLFGESIDSSKTE

3D structure

• PDB: 1r64 Structural Basis for Differences in Substrate Selectivity in Kex2 and Furin Protein Convertases
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D175 H213 N314 S385
• Catalytic site (residue number reindexed from 1): D55 H93 N194 S265
• 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	A	D176 H213 L246 I250 W273 G274 P275 D277 N314 D325 S385	D56 H93 L126 I130 W153 G154 P155 D157 N194 D205 S265
BS02	CA	A	D277 D320 E350	D157 D200 E230
BS03	CA	A	D135 D184 K224 N227 F229 G231	D15 D64 K104 N107 F109 G111
BS04	CA	A	T328 S330 S333 T335	T208 S210 S213 T215
BS05	K	A	A191 E192 G193 S194 N202 Y261	A71 E72 G73 S74 N82 Y141
BS06	K	A	T466 W467 A500	T346 W347 A380

Gene Ontology

Molecular Function

• GO:0004252 serine-type endopeptidase activity
• GO:0008236 serine-type peptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:1r64, PDBe:1r64, PDBj:1r64
• PDBsum: 1r64
• PubMed: 14992578
• UniProt: P13134|KEX2_YEAST Kexin (Gene Name=KEX2)