Structure of PDB 1gtl Chain 2

Receptor sequence
>1gtl2 (length=357) Species: 198803 (Bacillus sp. MN-32) [Search protein sequence]
AAPTAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDETSLAQYFASLG
VSAPQVVSVSVDGATNQPTGDPNGPDGEVELDIEVAGALAPGAKIAVYFA
PNTDAGFLNAITTAVHDPTHKPSIVSISWGGPEDSWAPASIAAMNRAFLD
AAALGVTVLAAAGDSGSTDGEQDGLYHVDFPAASPYVLACGGTRLVASAG
RIERETVWNDGPDGGSTGGGVSRIFPLPSWQERANVPPSANPGAGSGRGV
PDVAGNADPATGYEVVIDGETTVIGGTSAVAPLFAALVARINQKLGKPVG
YLNPTLYQLPPEVFHDITEGNNDIANRARIYQAGPGWDPCTGLGSPIGIR
LLQALLP
3D structure
PDB1gtl The 1.4 A Crystal Structure of Kumamolysin. A Thermostable Serine-Carboxyl-Type Proteinase
Chain2
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D164
Catalytic site (residue number reindexed from 1) D164
Enzyme Commision number ?
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 2 E78 N102 S128 W129 G130 G163 D164 D179 G276 T277 S278 E78 N102 S128 W129 G130 G163 D164 D179 G276 T277 S278
BS02 CA 2 D316 I317 G334 G336 D338 D316 I317 G334 G336 D338
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:1gtl, PDBe:1gtl, PDBj:1gtl
PDBsum1gtl
PubMed12057200
UniProtQ8RR56

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