Structure of PDB 3phm Chain A Binding Site BS03
Receptor Information
>3phm Chain A (length=310) Species:
10116
(Rattus norvegicus) [
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NECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFV
IDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARN
APPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLT
RVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTH
HLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCV
FTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFR
TIPAEANIPI
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
3phm Chain A Residue 358 [
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Receptor-Ligand Complex Structure
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PDB
3phm
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
H242 H244 M314
Binding residue
(residue number reindexed from 1)
H198 H200 M270
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)
H63 H64 Q126 H128 H198 H200 M270
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:3phm
,
PDBe:3phm
,
PDBj:3phm
PDBsum
3phm
PubMed
10504734
UniProt
P14925
|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)
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