1PHM

PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) FROM RAT

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 PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU A 357

Chain	Residue
A	HIS107
A	HIS108
A	HIS172

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 358

Chain	Residue
A	HOH360
A	HIS242
A	HIS244
A	MET314

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 359

Chain	Residue
A	HIS235
A	HIS305
A	AZI361
A	GOL362
A	HOH363

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AZI A 361

Chain	Residue
A	HIS235
A	PRO280
A	ASP282
A	HIS305
A	CU359
A	GOL362
A	HOH389
A	HOH465

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 362

Chain	Residue
A	HIS235
A	ASP282
A	HIS305
A	ASP312
A	CU359
A	AZI361
A	HOH363
A	HOH424
A	HOH433

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 601

Chain	Residue
A	LEU138
A	TYR139
A	THR148
A	LEU150
A	MET320
A	HOH398
A	HOH406
A	HOH409
A	HOH415

---

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 602

Chain	Residue
A	GLY113
A	ASN136
A	LEU138
A	PHE156
A	ARG157
A	GLY163
A	SER164
A	SER330
A	HOH364
A	HOH376

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 603

Chain	Residue
A	TYR205
A	GLN228
A	TYR229
A	LYS230
A	MET231
A	MET332
A	THR333
A	HOH562
A	HOH591

---

site_id	CUB
Number of Residues	3
Details	ACTIVE SITE RESIDUES R240,Y318,N316 HYDROGEN BOND TO PEPTIDYLGLYCINE SUBSTRATE.

Chain	Residue
A	ARG240
A	TYR318
A	ASN316

---

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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10504734","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15131304","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16100265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20958070","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23247335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36880254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YIP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E4Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DSJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10504734","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15131304","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16100265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20958070","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23247335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30271955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36880254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YIP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E4Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ALV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DSJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10504734","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15131304","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20958070","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23247335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30271955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36880254","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MIB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E4Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ALV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8DSJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1opm

Chain	Residue	Details
A	HIS242
A	GLN170
A	HIS108

---

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

---