Structure of PDB 1gtl Chain 2 Binding Site BS02

Receptor Information

>1gtl Chain 2 (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

Ligand ID

InChI

InChI=1S/Ca/q+2

InChIKey

BHPQYMZQTOCNFJ-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.341	[Ca++]
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Ca+2]

Formula

Name

CALCIUM ION

PDB chain

1gtl Chain 2 Residue 1358 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

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)	D316 I317 G334 G336 D338
Binding residue (residue number reindexed from 1)	D316 I317 G334 G336 D338
Annotation score	4

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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