Structure of PDB 5lrk Chain A

Receptor sequence
>5lrkA (length=304) Species: 9823 (Sus scrofa) [Search protein sequence]
GHSYEKYNNWETIEAWTKQVTSENPDLISRTAIGTTFLGNNIYLLKVGKP
GPNKPAIFMDCGFHAREWISHAFCQWFVREAVLTYGYESHMTEFLNKLDF
YVLPVLNIDGYIYTWTKNRMWRKTRSTNAGTTCIGTDPNRNFDAGWCTTG
ASTDPCDETYCGSAAESEKETKALADFIRNNLSSIKAYLTIHSYSQMILY
PYSYDYKLPENNAELNNLAKAAVKELATLYGTKYTYGPGATTIYPAAGGS
DDWAYDQGIKYSFTFELRDKGRYGFILPESQIQATCEETMLAIKYVTNYV
LGHL
3D structure
PDB5lrk Isolation, Co-Crystallization and Structure-Based Characterization of Anabaenopeptins as Highly Potent Inhibitors of Activated Thrombin Activatable Fibrinolysis Inhibitor (TAFIa).
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H69 E72 R127 H196 E270
Catalytic site (residue number reindexed from 1) H64 E67 R122 H192 E266
Enzyme Commision number 3.4.17.2: carboxypeptidase B.
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 H69 R71 M125 R127 N144 R145 E163 Y198 S207 Y248 D255 T268 E270 F279 H64 R66 M120 R122 N139 R140 E158 Y194 S203 Y244 D251 T264 E266 F275
BS02 ZN A H69 E72 H196 H64 E67 H192
Gene Ontology
Molecular Function
GO:0004181 metallocarboxypeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:5lrk, PDBe:5lrk, PDBj:5lrk
PDBsum5lrk
PubMed27604544
UniProtP09955|CBPB1_PIG Carboxypeptidase B (Gene Name=CPB1)

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