Structure of PDB 1hpg Chain A

Receptor sequence
>1hpgA (length=187) Species: 1911 (Streptomyces griseus) [Search protein sequence]
VLGGGAIYGGGSRCSAAFNVTKGGARYFVTAGHCTNISANWSASSGGSVV
GVREGTSFPTNDYGIVRYTDGSSPAGTVDLYNGSTQDISSAANAVVGQAI
KKSGSTTKVTSGTVTAVNVTVNYGDGPVYNMVRTTACSAGGDSGGAHFAG
SVALGIHSGSSGCSGTAGSAIHQPVTEALSAYGVTVY
3D structure
PDB1hpg A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 G193 S195 S214
Catalytic site (residue number reindexed from 1) H33 D62 G141 S143 S158
Enzyme Commision number 3.4.21.82: glutamyl endopeptidase II.
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 H57 Y171 S192 G192B G193 S195 H213 S214 G215 S216 S217 H33 Y123 S138 G140 G141 S143 H157 S158 G159 S160 S161
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:1hpg, PDBe:1hpg, PDBj:1hpg
PDBsum1hpg
PubMed8105890
UniProtQ07006|GLUP_STRGR Glutamyl endopeptidase 2 (Gene Name=sprE)

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