Structure of PDB 4e4z Chain A

Receptor sequence
>4e4zA (length=312) Species: 10116 (Rattus norvegicus) [Search protein sequence]
NECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFV
IDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARN
APPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLT
RVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTH
HLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCV
FTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFR
TIPAEANIPIPV
3D structure
PDB4e4z Coordination of peroxide to the Cu(M) center of peptidylglycine alpha-hydroxylating monooxygenase (PHM): structural and computational study.
ChainA
Resolution1.98 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CU A H107 H108 H172 H63 H64 H128
BS02 CU A H242 H244 M314 H198 H200 M270
BS03 PEO A E128 H244 M314 E84 H200 M270
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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Cellular Component
External links
PDB RCSB:4e4z, PDBe:4e4z, PDBj:4e4z
PDBsum4e4z
PubMed23247335
UniProtP14925|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)

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