4IW3

Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) in complex with elongation factor Tu (EF-Tu)

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	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003746	molecular_function	translation elongation factor activity
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006414	biological_process	translational elongation
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
J	0005506	molecular_function	iron ion binding
J	0008198	molecular_function	ferrous iron binding
J	0016491	molecular_function	oxidoreductase activity
J	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
J	0031418	molecular_function	L-ascorbic acid binding
J	0031543	molecular_function	peptidyl-proline dioxygenase activity
J	0046872	molecular_function	metal ion binding
J	0051213	molecular_function	dioxygenase activity
J	0071456	biological_process	cellular response to hypoxia
K	0000166	molecular_function	nucleotide binding
K	0000287	molecular_function	magnesium ion binding
K	0003746	molecular_function	translation elongation factor activity
K	0003924	molecular_function	GTPase activity
K	0005525	molecular_function	GTP binding
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0006412	biological_process	translation
K	0006414	biological_process	translational elongation
K	0016787	molecular_function	hydrolase activity
K	0046872	molecular_function	metal ion binding

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	HOH563

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE OGA A 402

Chain	Residue
A	HIS183
A	VAL185
A	ARG192
A	THR196
A	TRP198
A	MN401
A	HOH504
A	HOH540
A	HOH563
B	PRO54
A	HIS124
A	ASP126
A	TYR141
A	LEU154

---

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE GDP B 501

Chain	Residue
B	HIS20
B	ASP22
B	HIS23
B	GLY24
B	LYS25
B	THR26
B	THR27
B	ASN136
B	LYS137
B	ASP139
B	SER174
B	ALA175
B	ARG176
B	ARG176
B	MG502
B	HOH616

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 502

Chain	Residue
B	LYS25
B	THR26
B	CYS82
B	GDP501
B	HOH616

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG K 401

Chain	Residue
K	THR26
K	ASP81
K	CYS82
K	GDP402
K	HOH525
K	HOH536
K	HOH537

---

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GDP K 402

Chain	Residue
K	HIS20
K	VAL21
K	ASP22
K	HIS23
K	GLY24
K	LYS25
K	THR26
K	THR27
K	ASN136
K	LYS137
K	ASP139
K	LEU140
K	SER174
K	ALA175
K	ARG176
K	ARG176
K	MG401
K	HOH525
K	HOH537

---

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

Chain	Residue
J	HIS124
J	ASP126
J	HIS183
J	OGA402
J	HOH532

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE OGA J 402

Chain	Residue
J	TYR121
J	HIS124
J	ASP126
J	VAL139
J	TYR141
J	LEU154
J	HIS183
J	VAL185
J	ARG192
J	THR196
J	TRP198
J	MN401
J	HOH524
J	HOH532
J	HOH533
K	PRO54

---

Functional Information from PROSITE/UniProt

site_id	PS00301
Number of Residues	16
Details	G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DSapeEKaRGITIntA

Chain	Residue	Details
B	ASP51-ALA66

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI3
Number of Residues	14
Details	Region: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	8
Details	Region: {"description":"G2","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Region: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Region: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Region: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00118","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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