Structure of PDB 1qmu Chain A Binding Site BS01
Receptor Information
>1qmu Chain A (length=380) [
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QAVQPVDFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEI
SDNPGIHEAGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTD
LVQSTRIHIMPSMNPDGYEKSQEGDRGGTVGRNNSNNYDLNRNFPDQFFQ
VTDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGIAIYSK
SPDDAVFQQLALSYSKENKKMYQGSPCKDLYPTEYFPHGITNGAQWYNVP
GGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRSLLQFIKQVH
RGIWGFVLDATDGRGILNATISVADINHPVTTYKDGDYWRLLVQGTYKVT
ASARGYDPVTKTVEVDSKGGVQVNFTLSRT
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1qmu Chain A Residue 999 [
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Receptor-Ligand Complex Structure
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PDB
1qmu
Crystal Structure of Avian Carboxypeptidase D Domain II : A Prototype for the Regulatory Metallocarboxypeptidase Subfamily
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
H74 E77 H181
Binding residue
(residue number reindexed from 1)
H71 E74 H178
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.4.17.22
: metallocarboxypeptidase D.
Gene Ontology
Molecular Function
GO:0004180
carboxypeptidase activity
GO:0004181
metallocarboxypeptidase activity
GO:0008237
metallopeptidase activity
GO:0008270
zinc ion binding
GO:0046872
metal ion binding
Biological Process
GO:0006508
proteolysis
GO:0006518
peptide metabolic process
GO:0016485
protein processing
Cellular Component
GO:0005615
extracellular space
GO:0016020
membrane
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1qmu
,
PDBe:1qmu
,
PDBj:1qmu
PDBsum
1qmu
PubMed
10545093
UniProt
P83852
|CBPD_LOPSP Carboxypeptidase D (Fragment) (Gene Name=CPD)
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