Structure of PDB 2xs3 Chain A

Receptor sequence
>2xs3A (length=166) Species: 28112 (Tannerella forsythia) [Search protein sequence]
YVLQGSKWNKTTLKYYIYNSSSHLTTTERENAIRSAFALWSDKSTLSFIQ
VYNPNQADIKIKWEKGNHGDGYPFDGNTGILAHAFYPPPAGGNYAGHLHF
DDDENWSINGSGIDLITVAAHEIGHLLGIEHSNVSSALMYPYYTGIKRQL
DNDDCLAVWDLYGYPF
3D structure
PDB2xs3 The Structure of the Catalytic Domain of Tannerella Forsythia Karilysin Reveals It is a Bacterial Xenologue of Animal Matrix Metalloproteinases.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H155 E156 H159 H165
Catalytic site (residue number reindexed from 1) H121 E122 H125 H131
Enzyme Commision number 3.4.24.-
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 T112 H155 E156 H159 H165 P175 Y176 Y177 T78 H121 E122 H125 H131 P141 Y142 Y143
BS02 ZN A H102 D104 H117 H133 H68 D70 H83 H99
BS03 ZN A H155 H159 H165 H121 H125 H131
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0031012 extracellular matrix

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Molecular Function
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Cellular Component
External links
PDB RCSB:2xs3, PDBe:2xs3, PDBj:2xs3
PDBsum2xs3
PubMed21166898
UniProtD0EM77|KLY_TANFA Karilysin (Gene Name=kly)

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