Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4J25

Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0008198	molecular_function	ferrous iron binding
A	0016491	molecular_function	oxidoreductase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0031418	molecular_function	L-ascorbic acid binding
A	0031543	molecular_function	peptidyl-proline dioxygenase activity
A	0046872	molecular_function	metal ion binding
A	0051213	molecular_function	dioxygenase activity
A	0071456	biological_process	cellular response to hypoxia
B	0005506	molecular_function	iron ion binding
B	0008198	molecular_function	ferrous iron binding
B	0016491	molecular_function	oxidoreductase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0031418	molecular_function	L-ascorbic acid binding
B	0031543	molecular_function	peptidyl-proline dioxygenase activity
B	0046872	molecular_function	metal ion binding
B	0051213	molecular_function	dioxygenase activity
B	0071456	biological_process	cellular response to hypoxia
C	0005506	molecular_function	iron ion binding
C	0008198	molecular_function	ferrous iron binding
C	0016491	molecular_function	oxidoreductase activity
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0031418	molecular_function	L-ascorbic acid binding
C	0031543	molecular_function	peptidyl-proline dioxygenase activity
C	0046872	molecular_function	metal ion binding
C	0051213	molecular_function	dioxygenase activity
C	0071456	biological_process	cellular response to hypoxia
D	0005506	molecular_function	iron ion binding
D	0008198	molecular_function	ferrous iron binding
D	0016491	molecular_function	oxidoreductase activity
D	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D	0031418	molecular_function	L-ascorbic acid binding
D	0031543	molecular_function	peptidyl-proline dioxygenase activity
D	0046872	molecular_function	metal ion binding
D	0051213	molecular_function	dioxygenase activity
D	0071456	biological_process	cellular response to hypoxia
E	0005506	molecular_function	iron ion binding
E	0008198	molecular_function	ferrous iron binding
E	0016491	molecular_function	oxidoreductase activity
E	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
E	0031418	molecular_function	L-ascorbic acid binding
E	0031543	molecular_function	peptidyl-proline dioxygenase activity
E	0046872	molecular_function	metal ion binding
E	0051213	molecular_function	dioxygenase activity
E	0071456	biological_process	cellular response to hypoxia
F	0005506	molecular_function	iron ion binding
F	0008198	molecular_function	ferrous iron binding
F	0016491	molecular_function	oxidoreductase activity
F	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
F	0031418	molecular_function	L-ascorbic acid binding
F	0031543	molecular_function	peptidyl-proline dioxygenase activity
F	0046872	molecular_function	metal ion binding
F	0051213	molecular_function	dioxygenase activity
F	0071456	biological_process	cellular response to hypoxia
G	0005506	molecular_function	iron ion binding
G	0008198	molecular_function	ferrous iron binding
G	0016491	molecular_function	oxidoreductase activity
G	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
G	0031418	molecular_function	L-ascorbic acid binding
G	0031543	molecular_function	peptidyl-proline dioxygenase activity
G	0046872	molecular_function	metal ion binding
G	0051213	molecular_function	dioxygenase activity
G	0071456	biological_process	cellular response to hypoxia
H	0005506	molecular_function	iron ion binding
H	0008198	molecular_function	ferrous iron binding
H	0016491	molecular_function	oxidoreductase activity
H	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
H	0031418	molecular_function	L-ascorbic acid binding
H	0031543	molecular_function	peptidyl-proline dioxygenase activity
H	0046872	molecular_function	metal ion binding
H	0051213	molecular_function	dioxygenase activity
H	0071456	biological_process	cellular response to hypoxia

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 401

Chain	Residue
A	HIS124
A	ASP126
A	HIS183
A	OGA402
A	HOH503

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE OGA A 402

Chain	Residue
A	LEU154
A	HIS183
A	VAL185
A	ARG192
A	THR196
A	MN401
A	HOH503
A	HOH579
A	TYR121
A	HIS124
A	ASP126
A	TYR141

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 401

Chain	Residue
B	HIS124
B	ASP126
B	HIS183
B	OGA402
B	HOH518

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OGA B 402

Chain	Residue
B	HIS124
B	ASP126
B	TYR141
B	LEU154
B	HIS183
B	VAL185
B	ARG192
B	SER194
B	THR196
B	TRP198
B	MN401
B	HOH518
B	HOH561

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 401

Chain	Residue
C	HIS124
C	ASP126
C	HIS183
C	OGA402
C	HOH508

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE OGA C 402

Chain	Residue
C	TYR121
C	HIS124
C	ASP126
C	TYR141
C	LEU154
C	HIS183
C	VAL185
C	ARG192
C	THR196
C	TRP198
C	MN401
C	HOH508
C	HOH536
C	HOH575

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 401

Chain	Residue
D	HIS124
D	ASP126
D	HIS183
D	OGA402
D	HOH505

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OGA D 402

Chain	Residue
D	TYR121
D	HIS124
D	ASP126
D	TYR141
D	LEU154
D	HIS183
D	ARG192
D	SER194
D	THR196
D	MN401
D	HOH505
D	HOH546
D	HOH580

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN E 401

Chain	Residue
E	HIS124
E	ASP126
E	HIS183
E	OGA402
E	HOH509

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE OGA E 402

Chain	Residue
E	TYR121
E	HIS124
E	ASP126
E	TYR141
E	HIS183
E	VAL185
E	ARG192
E	SER194
E	THR196
E	TRP198
E	MN401
E	HOH504
E	HOH507
E	HOH509
E	HOH524

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN F 401

Chain	Residue
F	HIS124
F	ASP126
F	HIS183
F	OGA402
F	HOH506

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE OGA F 402

Chain	Residue
F	HIS124
F	ASP126
F	TYR141
F	HIS183
F	VAL185
F	ARG192
F	THR196
F	MN401
F	HOH506
F	HOH508
F	TYR115
F	TYR121

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN G 401

Chain	Residue
G	HIS124
G	ASP126
G	HIS183
G	OGA402
G	HOH505

site_id	BC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE OGA G 402

Chain	Residue
G	TYR115
G	TYR121
G	HIS124
G	ASP126
G	VAL139
G	TYR141
G	HIS183
G	VAL185
G	ARG192
G	THR196
G	TRP198
G	MN401
G	HOH505
G	HOH509
G	HOH539

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN H 401

Chain	Residue
H	HIS124
H	ASP126
H	HIS183
H	OGA402
H	HOH502

site_id	BC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE OGA H 402

Chain	Residue
H	TYR115
H	TYR121
H	HIS124
H	ASP126
H	VAL139
H	TYR141
H	LEU154
H	HIS183
H	ARG192
H	THR196
H	TRP198
H	MN401
H	HOH502
H	HOH507
H	HOH528

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)