Structure of PDB 6ala Chain C Binding Site BS01
Receptor Information
>6ala Chain C (length=304) Species:
10116
(Rattus norvegicus) [
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PVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRAS
MDTVHAMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPK
GVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQPLIA
GMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKVVSG
YRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEGRTE
ATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANI
PIPV
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
6ala Chain C Residue 1001 [
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Receptor-Ligand Complex Structure
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PDB
6ala
Effects of copper occupancy on the conformational landscape of peptidylglycine alpha-hydroxylating monooxygenase.
Resolution
2.59 Å
Binding residue
(original residue number in PDB)
H107 H242 H244
Binding residue
(residue number reindexed from 1)
H55 H190 H192
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)
H55 A56 Q118 H120 H190 H192 M262
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6ala
,
PDBe:6ala
,
PDBj:6ala
PDBsum
6ala
PubMed
30271955
UniProt
P14925
|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)
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