Structure of PDB 1gtl Chain 1 Binding Site BS01

Receptor Information

>1gtl Chain 1 (length=357) Species: 198803 (Bacillus sp. MN-32) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

AAPTAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDETSLAQYFASLG
VSAPQVVSVSVDGATNQPTGDPNGPDGEVELDIEVAGALAPGAKIAVYFA
PNTDAGFLNAITTAVHDPTHKPSIVSISWGGPEDSWAPASIAAMNRAFLD
AAALGVTVLAAAGDSGSTDGEQDGLYHVDFPAASPYVLACGGTRLVASAG
RIERETVWNDGPDGGSTGGGVSRIFPLPSWQERANVPPSANPGAGSGRGV
PDVAGNADPATGYEVVIDGETTVIGGTSAVAPLFAALVARINQKLGKPVG
YLNPTLYQLPPEVFHDITEGNNDIANRARIYQAGPGWDPCTGLGSPIGIR
LLQALLP

Ligand information

>1gtl Chain 3 (length=3) Species: 32630 (synthetic construct) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

IPF

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1gtl The 1.4 A Crystal Structure of Kumamolysin. A Thermostable Serine-Carboxyl-Type Proteinase
Resolution	2.8 Å
Binding residue (original residue number in PDB)	E78 N102 S128 W129 G130 G163 D164 D179 G276 T277 S278
Binding residue (residue number reindexed from 1)	E78 N102 S128 W129 G130 G163 D164 D179 G276 T277 S278

Enzymatic activity

Catalytic site (original residue number in PDB)	D164
Catalytic site (residue number reindexed from 1)	D164
Enzyme Commision number	?

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
PDBsum	1gtl
PubMed	12057200
UniProt	Q8RR56

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