Structure of PDB 1r0r Chain E

Receptor sequence
>1r0rE (length=274) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASF
VAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGS
GSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYARGVVVVA
AAGNSGNSGSTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAP
GAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLS
STATYLGSSFYYGKGLINVEAAAQ
3D structure
PDB1r0r Structure and energetics of protein-protein interactions: the role of conformational heterogeneity in OMTKY3 binding to serine proteases
ChainE
Resolution1.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S221
Catalytic site (residue number reindexed from 1) S220
Enzyme Commision number 3.4.21.62: subtilisin.
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 CA E A37 S38 H39 L42 A37 S38 H39 L42
BS02 CA E Q2 D41 L75 N77 T79 V81 Q2 D41 L74 N76 T78 V80
BS03 CA E G193 A194 L196 S260 G192 A193 L195 S259
BS04 CA E A169 Y171 V174 A168 Y170 V173
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:1r0r, PDBe:1r0r, PDBj:1r0r
PDBsum1r0r
PubMed12888355
UniProtP00780|SUBC_BACLI Subtilisin Carlsberg (Gene Name=subC)

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