Structure of PDB 6i6z Chain A

Receptor sequence
>6i6zA (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
STDTFNYATYHTLEEIYDFLDLLVAENPHLVSKIQIGNTYEGRPIYVLKF
STGGSKRPAIWIDTGIHSREWVTQASGVWFAKKITQDYGQDAAFTAILDT
LDIFLEIVTNPDGFAFTHSTNRMWRKTRSHTAGSLCIGVDPNRNWDAGFG
LSGASSNPCSETYHGKFANSEVEVKSIVDFVKDHGNIKAFISIHSYSQLL
MYPYGYKTEPVPDQDELDQLSKAAVTALASLYGTKFNYGSIIKAIYQASG
STIDWTYSQGIKYSFTFELRDTGRYGFLLPASQIIPTAKETWLALLTIME
HTLNHP
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.
ChainA
Resolution1.72 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H179 E182 R237 H306 E380
Catalytic site (residue number reindexed from 1) H67 E70 R125 H194 E268
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 A H179 R237 N254 R255 T274 H306 Y308 I353 Y358 T378 E380 H67 R125 N142 R143 T162 H194 Y196 I241 Y246 T266 E268 BindingDB: Ki=0.530000nM
BS02 ZN A H179 E182 H306 H67 E70 H194
Gene Ontology
Molecular Function
GO:0004181 metallocarboxypeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6i6z, PDBe:6i6z, PDBj:6i6z
PDBsum6i6z
PubMed30688452
UniProtP15085|CBPA1_HUMAN Carboxypeptidase A1 (Gene Name=CPA1)

[Back to BioLiP]