Structure of PDB 6nck Chain A Binding Site BS01
Receptor Information
>6nck Chain A (length=300) Species:
10116
(Rattus norvegicus) [
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CPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRA
SMDTVHAMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLP
KGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQPLI
AGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKVVS
GYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEGRT
EATHISSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANIPI
Ligand information
Ligand ID
CU
InChI
InChI=1S/Cu/q+2
InChIKey
JPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341
[Cu++]
Formula
Cu
Name
COPPER (II) ION
ChEMBL
DrugBank
DB14552
ZINC
PDB chain
6nck Chain A Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
6nck
Getting the Most Out of Your Crystals: Data Collection at the New High-Flux, Microfocus MX Beamlines at NSLS-II.
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
H242 H244 M314
Binding residue
(residue number reindexed from 1)
H191 H193 M260
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H107 A108 Q170 H172 H242 H244 M314
Catalytic site (residue number reindexed from 1)
H56 A57 Q119 H121 H191 H193 M260
Enzyme Commision number
1.14.17.3
: peptidylglycine monooxygenase.
4.3.2.5
: peptidylamidoglycolate lyase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0004497
monooxygenase activity
GO:0005507
copper ion binding
GO:0016715
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
Biological Process
GO:0006518
peptide metabolic process
Cellular Component
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:6nck
,
PDBe:6nck
,
PDBj:6nck
PDBsum
6nck
PubMed
30704096
UniProt
P14925
|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)
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