Structure of PDB 2xrm Chain A

Receptor sequence
>2xrmA (length=301) Species: 79880 (Shouchella clausii) [Search protein sequence]
SEVPMGVEIVEAPAVWRASAKGAGQIIGVIDTGCQVDHPDLAERIIGGVN
LTTDYGGDETNFSDNNGHGTHVAGTVAAAETGSGVVGVAPKADLFIIKAL
SGDGSGEMGWIAKAIRYAVDWRGPKGEQMRIITMSLGGPTDSEELHDAVK
YAVSNNVSVVCAAGNEGDGREDTNEFAYPAAYNEVIAVGAVDFDLRLSDF
TNTNEEIDIVAPGVGIKSTYLDSGYAELSGTAMAAPHVAGALALIINLAE
DAFKRSLSETEIYAQLVRRATPIGFTAQAEGNGFLTLDLVERITGQFTEK
G
3D structure
PDB2xrm Regulation of an Intracellular Subtilisin Protease Activity by a Short Propeptide Sequence Through an Original Combined Dual Mechanism.
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D49 H86 N183 A250
Catalytic site (residue number reindexed from 1) D31 H68 N165 A232
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 A D186 R188 T191 E193 T221 D168 R170 T173 E175 T203
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2xrm, PDBe:2xrm, PDBj:2xrm
PDBsum2xrm
PubMed21307308
UniProtD0AB41

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