Structure of PDB 6i6z Chain B

Receptor sequence
>6i6zB (length=307) Species: 9606 (Homo sapiens) [Search protein sequence]
RSTDTFNYATYHTLEEIYDFLDLLVAENPHLVSKIQIGNTYEGRPIYVLK
FSTGGSKRPAIWIDTGIHSREWVTQASGVWFAKKITQDYGQDAAFTAILD
TLDIFLEIVTNPDGFAFTHSTNRMWRKTRSHTAGSLCIGVDPNRNWDAGF
GLSGASSNPCSETYHGKFANSEVEVKSIVDFVKDHGNIKAFISIHSYSQL
LMYPYGYKTEPVPDQDELDQLSKAAVTALASLYGTKFNYGSIIKAIYQAS
GSTIDWTYSQGIKYSFTFELRDTGRYGFLLPASQIIPTAKETWLALLTIM
EHTLNHP
3D structure
PDB6i6z Synthesis and Structural/Functional Characterization of Selective M14 Metallocarboxypeptidase Inhibitors Based on Phosphinic Pseudopeptide Scaffold: Implications on the Design of Specific Optical Probes.
ChainB
Resolution1.72 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H179 E182 R237 H306 E380
Catalytic site (residue number reindexed from 1) H68 E71 R126 H195 E269
Enzyme Commision number 3.4.17.1: carboxypeptidase A.
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 TJE B H179 R181 R237 N254 R255 H306 Y308 I353 Y358 T378 E380 H68 R70 R126 N143 R144 H195 Y197 I242 Y247 T267 E269 BindingDB: Ki=0.530000nM
BS02 ZN B H179 E182 H306 H68 E71 H195
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:6i6z, PDBe:6i6z, PDBj:6i6z
PDBsum6i6z
PubMed30688452
UniProtP15085|CBPA1_HUMAN Carboxypeptidase A1 (Gene Name=CPA1)

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