Structure of PDB 1dtd Chain A

Receptor sequence
>1dtdA (length=303) Species: 9606 (Homo sapiens) [Search protein sequence]
FNFGAYHTLEEISQEMDNLVAEHPGLVSKVNIGSSFENRPMNVLKFSTGG
DKPAIWLDAGIHAREWVTQATALWTANKIVSDYGKDPSITSILDALDIFL
LPVTNPDGYVFSQTKNRMWRKTRSKVSAGSLCVGVDPNRNWDAGFGGPGA
SSNPCSDSYHGPSANSEVEVKSIVDFIKSHGKVKAFIILHSYSQLLMFPY
GYKCTKLDDFDELSEVAQKAAQSLSRLHGTKYKVGPICSVIYQASGGSID
WSYDYGIKYSFAFELRDTGRYGFLLPARQILPTAEETWLGLKAIMEHVRD
HPY
3D structure
PDB1dtd Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2.
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H424 E427 R482 H552 E626
Catalytic site (residue number reindexed from 1) H62 E65 R120 H190 E264
Enzyme Commision number 3.4.17.15: carboxypeptidase A2.
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 ZN A H424 E427 H552 H62 E65 H190
BS02 GLU A H424 N500 R501 H552 Y604 E626 H62 N138 R139 H190 Y242 E264
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:1dtd, PDBe:1dtd, PDBj:1dtd
PDBsum1dtd
PubMed10742178
UniProtP48052|CBPA2_HUMAN Carboxypeptidase A2 (Gene Name=CPA2)

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