Structure of PDB 3ro0 Chain C

Receptor sequence
>3ro0C (length=207) Species: 1390 (Bacillus amyloliquefaciens) [Search protein sequence]
MEKKVLLTGFDPFGGETVNPSWEAVKRLNGAAEGPASIVSEQVPTVFYKS
LAVLREAMKKHQPDIIICVGQAGGRMQITPERVAINLNEARIPDNEGNQP
VGEDISQGGPAAYWTGLPIKRIVEEIKKEGIPAAVSYTAGTFVCNHLFYG
LMDEISRHHPHIRGGFIHIPYIPEQTLQKSAPSLSLDHITKALKIAAVTA
AAHEDDI
3D structure
PDB3ro0 Terpyridine platinum(II) complexes inhibit cysteine proteases by binding to active-site cysteine.
ChainC
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) E81 R91 C144 H168
Catalytic site (residue number reindexed from 1) E81 R91 C144 H168
Enzyme Commision number 3.4.19.3: pyroglutamyl-peptidase I.
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 TPT C F10 F13 T45 A139 F142 C144 H168 F10 F13 T45 A139 F142 C144 H168
Gene Ontology
Molecular Function
GO:0008234 cysteine-type peptidase activity
GO:0016920 pyroglutamyl-peptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:3ro0, PDBe:3ro0, PDBj:3ro0
PDBsum3ro0
PubMed21875148
UniProtP46107|PCP_BACAM Pyrrolidone-carboxylate peptidase (Gene Name=pcp)

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