Structure of PDB 3mlk Chain A Binding Site BS01
Receptor Information
>3mlk Chain A (length=306) Species:
10116
(Rattus norvegicus) [
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ECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVI
DFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNA
PPTRLPKGVGFRVGGETGSKYFVLQVHYGDIRDNHKDCSGVSVHLTRVPQ
PLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGK
VVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGE
GRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPA
EANIPI
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
3mlk Chain A Residue 358 [
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Receptor-Ligand Complex Structure
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PDB
3mlk
Differential reactivity between two copper sites in peptidylglycine alpha-hydroxylating monooxygenase
Resolution
3.1 Å
Binding residue
(original residue number in PDB)
H242 H244
Binding residue
(residue number reindexed from 1)
H194 H196
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H107 H108 Q170 H172 H242 H244 M314
Catalytic site (residue number reindexed from 1)
H62 H63 Q125 H127 H194 H196 M266
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:3mlk
,
PDBe:3mlk
,
PDBj:3mlk
PDBsum
3mlk
PubMed
20958070
UniProt
P14925
|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)
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