5WM0

Crystal structure of apo wild type peptidylglycine alpha-hydroxylating monooxygenase (PHM) soaked with peptide (peptide not observed)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004497	molecular_function	monooxygenase activity
A	0005507	molecular_function	copper ion binding
A	0006518	biological_process	peptide metabolic process
A	0016020	cellular_component	membrane
A	0016715	molecular_function	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

Functional Information from PROSITE/UniProt

site_id	PS00084
Number of Residues	8
Details	CU2_MONOOXYGENASE_1 Copper type II, ascorbate-dependent monooxygenases signature 1. HHMllFgC

Chain	Residue	Details
A	HIS107-CYS114

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site_id	PS00085
Number of Residues	13
Details	CU2_MONOOXYGENASE_2 Copper type II, ascorbate-dependent monooxygenases signature 2. HvFayrvHTHhlG

Chain	Residue	Details
A	HIS235-GLY247

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	830
Details	TOPO_DOM: Intragranular => ECO:0000255

Chain	Residue	Details
A	PHE36-GLY866

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site_id	SWS_FT_FI2
Number of Residues	23
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
A	VAL867-ILE890

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site_id	SWS_FT_FI3
Number of Residues	85
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
A	ARG891-SER976

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site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:10504734, ECO:0007744|PDB:1OPM, ECO:0007744|PDB:3PHM

Chain	Residue	Details
A	HIS107
A	HIS108
A	HIS172
A	HIS242
A	HIS244
A	MET314

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site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:19604476, ECO:0007744|PDB:3FVZ, ECO:0007744|PDB:3FW0

Chain	Residue	Details
A	VAL520
A	LEU587
A	ASP787

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site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:19604476, ECO:0007744|PDB:3FW0

Chain	Residue	Details
A	ARG533
A	TYR654
A	ARG706

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site_id	SWS_FT_FI7
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:19604476, ECO:0007744|PDB:3FVZ

Chain	Residue	Details
A	HIS585
A	HIS690
A	HIS786

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site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19021

Chain	Residue	Details
A	SER921
A	SER932

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site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	SER945
A	SER949
A	SER961

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site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19021

Chain	Residue	Details
A	THR946

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site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	THR959

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site_id	SWS_FT_FI12
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2211657

Chain	Residue	Details
A	ASN765

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 135

Chain	Residue	Details
A	HIS107	metal ligand
A	HIS108	hydrogen bond donor, metal ligand, single electron acceptor, single electron donor, single electron relay
A	GLN170	hydrogen bond acceptor, single electron acceptor, single electron donor, single electron relay
A	HIS172	metal ligand
A	HIS242	metal ligand
A	HIS244	metal ligand
A	MET314	metal ligand

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